Pyruvate Kinase - Revision history

Alexander Berchansky at 09:44, 11 September 2022

2022-09-11T09:44:54Z

← Older revision		Revision as of 09:44, 11 September 2022
Line 8:		Line 8:

	==Mechanism==		==Mechanism==
	~~[[Image:Pyruvatekinasemechanism.gif\| left \| 500px]]~~
	~~<ref>{{website1\| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?\|url=http://www.sportsci.org/jour/0102/rar.htm\|}}</ref>~~
	<scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates one K+ and two Mg2+ cations to be used in two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=502\|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=503\|}}</ref>.		<scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates one K+ and two Mg2+ cations to be used in two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=502\|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=503\|}}</ref>.

Michal Harel at 08:20, 8 December 2019

2019-12-08T08:20:46Z

← Older revision		Revision as of 08:20, 8 December 2019
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	</StructureSection>		</StructureSection>
	~~==3D structures of pyruvate kinase==~~

	~~Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}~~
	~~{{#tree:id=OrganizedByTopic\|openlevels=0\|~~

	*Pyruvate kinase

	**[[3bjf]], [[3bjt]], [[1t5a]], [[1zjh]], [[3srf]], [[3srh]] - hPyK M1/M2 - human<br />
	**[[4wj8]], [[4qg6]], [[4qg8]], [[4qg9]], [[4qgc]], [[3g2g]], [[4yj5]], [[6b6u]] - hPyK M1/M2 (mutant)<br />
	**[[2vgb]] – hPyK R/L<br />
	**[[2vgf]], [[2vgg]], [[2vgi]] - hPyK R/L (mutant) <br />
	**[[6nn5]], [[6nn7]], [[6nn8]] – hPyK PKLR (mutant)<br />
	**[[1pkm]], [[1pyk]] – PyK – cat<br />
	**[[1f3w]] – rPyK – rabbit<br />
	**[[1f3x]] - rPyK (mutant) <br />
	**[[1pky]], [[4yng]] – EcPyK - ''Eschericia coli''<br />
	**[[1e0t]], [[1e0u]] - EcPyK (mutant) <br />
	**[[3t05]], [[3t0t]] – SaPyK – ''Staphylococcus aureus''<br />
	**[[3qtg]] – PyK – ''Pyrobaculum aerophilum''<br />
	**[[4krz]] - TcPyK – ''Trypanosoma cruzei''<br />
	**[[5wrp]] - MtPyK – ''Mycobacterium tuberculosis''<br />
	**[[3hqn]], [[3e0w]], [[1pkl]] – LmPyK – ''Leishmania mexicana''<br />
	**[[3khd]] – PyK – ''Plasmodium falciparum''<br />
	**[[3gg8]], [[3eoe]] – PyK – ''Toxoplasma gondii''<br />
	**[[3ma8]], [[4drs]] – PyK – ''Cryptosporidium parvum''<br />
	**[[2e28]] - PyK (mutant) – ''Geobacillus stearothermophilus''<br />

	*Pyruvate kinase binary complex

	**[[4b2d]] - hPyK M1/M2 + fructose bisphosphate<br />
	**[[4rpp]] - hPyK M2 (mutant) + fructose bisphosphate<br />
	**[[4fxj]] - hPyK M1/M2 + phenylalanine<br />
	**[[6gg3]] - hPyK M2 + alanine<br />
	**[[6gg4]] - hPyK M2 + phenylalanine<br />
	**[[6gg5]] - hPyK M2 + tryptophan<br />
	**[[6gg6]] - hPyK M2 + serine<br />
	**[[6nub]] - hPyK M2 (mutant) + serine<br />
	**[[6nu1]] - hPyK M2 + cysteine<br />
	**[[6nu5]] - hPyK M2 (mutant) + cysteine<br />
	**[[6ech]], [[6eck]] - PyK PKLR + fructose bisphosphate - rat<br />
	**[[5x1v]], [[5x1w]] - hPyK M2 + inhibitor<br />
	[[4rpp]] - hPyK M2 (mutant) + fructose bisphosphate<br />[[3qv9]] – TcPyK + Ponceau S <br />
	**[[3qv6]] – LmPyK + acid blue 80<br />
	**[[3e0v]] – LmPyK + sulfate<br />
	**[[3hqq]] - LmPyK + fructose bisphosphate<br />
	**[[3qv8]] – LmPyK + benzothiazole<br />
	**[[3pp7]] – LmPyK + suramin<br />
	**[[3is4]], [[3ktx]] – LmPyK + pyrenetetrasulfonic acid<br />
	**[[3t07]] – SaPyK + bis-indole alkaloid<br />
	**[[4hyw]] – TbPyK + fructose bisphosphate – ''Trypanosoma brucei''<br />
	**[[5ws8]] - MtPyK + oxalate<br />
	**[[6p0y]] - CpPyK + ADP<br />

	*Pyruvate kinase higher complex

	**[[3me3]] – hPyK M1/M2 + aniline derivative + fructose bisphosphate<br />
	**[[4g1n]] - hPyK M1/M2 + pyridazine derivative + oxalate<br />
	**[[3h6o]] - hPyK M1/M2 + pyridazine derivative + fructose bisphosphate<br />
	**[[3gqy]], [[3gr4]], [[3u2z]] - hPyK M1/M2 + piperazine derivative + fructose bisphosphate<br />
	**[[5x0i]] - hPyK M2 (mutant) + serine + fructose bisphosphate<br />
	**[[5x1v]], [[5x1w]] - hPyK M2 + activator + fructose bisphosphate<br />
	**[[4jpg]] - hPyK M1/M2 + pyrimidine derivative + fructose bisphosphate<br />
	**[[3srd]] - hPyK M1/M2 + oxalate + fructose bisphosphate<br />
	**[[4fxf]] - hPyK M1/M2 + oxalate + ATP + fructose bisphosphate<br />
	**[[4ima]], [[4ip7]] - hPyK L (mutant) + citrate + adenosine + fructose bisphosphate<br />
	**[[3n25]] – rPyK M1/M2 + proline + Mn + pyruvate<br />
	**[[2g50]] - rPyK M1/M2 + alanine + Mn + pyruvate<br />
	**[[1pkn]] - rPyK + Mn + pyruvate<br />
	**[[1aqf]] – rPyK + Mg + phospholactate<br />
	**[[1a49]], [[1a5u]] - rPyK + ATP + oxalate<br />
	**[[1a3w]] – yPyK + Mn + phosphoglycolic acid + fructose bisphosphate – yeast<br />
	**[[1a3x]] - yPyK + Mn + phosphoglycolic acid<br />
	**[[4hyv]] – TbPyK + phosphoenolpyruvate + fructose bisphosphate <br />
	**[[4kct]] – TbPyK + pyruvate + fructose bisphosphate <br />
	**[[4kcu]] – TbPyK + malate + fructose bisphosphate <br />
	**[[4kcv]] – TbPyK + oxoglutarate + fructose bisphosphate <br />
	**[[4kcw]] – TbPyK + oxalate + fructose bisphosphate <br />
	**[[4ks0]] – TcPyK + oxalate + fructose bisphosphate <br />
	**[[5ws9]] – MtPyK + oxalate + AMP + ATP <br />
	**[[5wsa]] – MtPyK + oxalate + glucose-6-phosphate <br />
	**[[5wsb]], [[5wsc]] – MtPyK + oxalate + glucose-6-phosphate + AMP<br />
	**[[6ito]] – MtPyK + oxalate + ribose-5-phosphate + AMP<br />
	**[[3hqo]] – LmPyK + ATP + oxalate<br />
	**[[3hqp]] - LmPyK + ATP + oxalate + fructose bisphosphate<br />
	**[[3qv7]] – LmPyK + acid blue 25 + Ponceau S<br />
	**[[3srk]] – LmPyK + saccharine + inhibitor<br />
	**[[6qxl]] – PyK + malonate + glucose-6-phosphate + Mg – ''Pseudomonas aerugnosa''<br />

	}}




	==Additional Resources==		==Additional Resources==

Michal Harel at 08:19, 8 December 2019

2019-12-08T08:19:31Z

← Older revision		Revision as of 08:19, 8 December 2019
Line 41:		Line 41:
	Red blood cells, in a state of pyruvate kinase deficiency, rapidly become deficient in ATP and can undergo hemolysis.This is transmitted as an autosomal recessive trit. The severity of hemolysis is extremely variable such as a mild case to life-threatening neonatal anaemia requiring transfusions. Over one hundred eighty different mutations have been discovered in relation to this deficiency with most being autosomal recessive, but a few strands are autosomal dominant. The deficiency causes red blood cells to deform into echinocytes on peripheral blood smears. This causes the buildup of reaction intermediates which can also increase the level of 2,3-bisphosphoglycerate in the cells. This causes a rightward shift in the hemoglobin oxygen saturation curve, which means that there is a decreased oxygen affinity for the hemoglobin and earlier oxygen unloading than under normal conditions		Red blood cells, in a state of pyruvate kinase deficiency, rapidly become deficient in ATP and can undergo hemolysis.This is transmitted as an autosomal recessive trit. The severity of hemolysis is extremely variable such as a mild case to life-threatening neonatal anaemia requiring transfusions. Over one hundred eighty different mutations have been discovered in relation to this deficiency with most being autosomal recessive, but a few strands are autosomal dominant. The deficiency causes red blood cells to deform into echinocytes on peripheral blood smears. This causes the buildup of reaction intermediates which can also increase the level of 2,3-bisphosphoglycerate in the cells. This causes a rightward shift in the hemoglobin oxygen saturation curve, which means that there is a decreased oxygen affinity for the hemoglobin and earlier oxygen unloading than under normal conditions
	<ref>PMID:17360088</ref>.		<ref>PMID:17360088</ref>.

			==3D structures of pyruvate kinase==
			[[Pyruvate kinase 3D structures]]

	</StructureSection>		</StructureSection>
	==3D structures of pyruvate kinase==		==3D structures of pyruvate kinase==
Line 49:		Line 53:
	*Pyruvate kinase		*Pyruvate kinase

	**[[3hqn]], [[3e0w]], [[1pkl]] – LmPyK – ''Leishmania mexicana''<br />
	**[[3khd]] – PyK – ''Plasmodium falciparum''<br />
	**[[3gg8]], [[3eoe]] – PyK – ''Toxoplasma gondii''<br />
	**[[3bjf]], [[3bjt]], [[1t5a]], [[1zjh]], [[3srf]], [[3srh]] - hPyK M1/M2 - human<br />		**[[3bjf]], [[3bjt]], [[1t5a]], [[1zjh]], [[3srf]], [[3srh]] - hPyK M1/M2 - human<br />
	**[[4wj8]], [[4qg6]], [[4qg8]], [[4qg9]], [[4qgc]], [[3g2g]], [[4yj5]] - hPyK M1/M2 (mutant)<br />		**[[4wj8]], [[4qg6]], [[4qg8]], [[4qg9]], [[4qgc]], [[3g2g]], [[4yj5]], [[6b6u]] - hPyK M1/M2 (mutant)<br />
	**[[2vgb]] – hPyK R/L<br />		**[[2vgb]] – hPyK R/L<br />
	**[[2vgf]], [[2vgg]], [[2vgi]] - hPyK R/L (mutant) <br />		**[[2vgf]], [[2vgg]], [[2vgi]] - hPyK R/L (mutant) <br />
	**[[~~3ma8~~]], [[~~4drs~~]] – ~~PyK – ''Cryptosporidium parvum''~~<br />		**[[6nn5]], [[6nn7]], [[6nn8]] – hPyK PKLR (mutant)<br />
	**[[~~2e28~~]] - PyK ~~(mutant)~~ – ~~''Geobacillus stearothermophilus''~~<br />		**[[1pkm]], [[1pyk]] – PyK – cat<br />
	**[[1f3w]] – rPyK – rabbit<br />		**[[1f3w]] – rPyK – rabbit<br />
	**[[1f3x]] - rPyK (mutant) <br />		**[[1f3x]] - rPyK (mutant) <br />
	**[[1pky]], [[4yng]] – EcPyK - ''Eschericia coli''<br />		**[[1pky]], [[4yng]] – EcPyK - ''Eschericia coli''<br />
	**[[1e0t]], [[1e0u]] - EcPyK (mutant) <br />		**[[1e0t]], [[1e0u]] - EcPyK (mutant) <br />
	**[[1pkm]], [[1pyk]] – PyK – cat<br />
	**[[3t05]], [[3t0t]] – SaPyK – ''Staphylococcus aureus''<br />		**[[3t05]], [[3t0t]] – SaPyK – ''Staphylococcus aureus''<br />
	**[[3qtg]] – PyK – ''Pyrobaculum aerophilum''<br />		**[[3qtg]] – PyK – ''Pyrobaculum aerophilum''<br />
	**[[4krz]] - TcPyK – ''Trypanosoma cruzei''<br />		**[[4krz]] - TcPyK – ''Trypanosoma cruzei''<br />
	**[[5wrp]] - MtPyK – ''Mycobacterium tuberculosis''<br />		**[[5wrp]] - MtPyK – ''Mycobacterium tuberculosis''<br />
			**[[3hqn]], [[3e0w]], [[1pkl]] – LmPyK – ''Leishmania mexicana''<br />
			**[[3khd]] – PyK – ''Plasmodium falciparum''<br />
			**[[3gg8]], [[3eoe]] – PyK – ''Toxoplasma gondii''<br />
			**[[3ma8]], [[4drs]] – PyK – ''Cryptosporidium parvum''<br />
			**[[2e28]] - PyK (mutant) – ''Geobacillus stearothermophilus''<br />

	*Pyruvate kinase binary complex		*Pyruvate kinase binary complex

	**[[3qv9]] – TcPyK + Ponceau S <br />		**[[4b2d]] - hPyK M1/M2 + fructose bisphosphate<br />
			**[[4rpp]] - hPyK M2 (mutant) + fructose bisphosphate<br />
			**[[4fxj]] - hPyK M1/M2 + phenylalanine<br />
			**[[6gg3]] - hPyK M2 + alanine<br />
			**[[6gg4]] - hPyK M2 + phenylalanine<br />
			**[[6gg5]] - hPyK M2 + tryptophan<br />
			**[[6gg6]] - hPyK M2 + serine<br />
			**[[6nub]] - hPyK M2 (mutant) + serine<br />
			**[[6nu1]] - hPyK M2 + cysteine<br />
			**[[6nu5]] - hPyK M2 (mutant) + cysteine<br />
			**[[6ech]], [[6eck]] - PyK PKLR + fructose bisphosphate - rat<br />
			**[[5x1v]], [[5x1w]] - hPyK M2 + inhibitor<br />
			[[4rpp]] - hPyK M2 (mutant) + fructose bisphosphate<br />[[3qv9]] – TcPyK + Ponceau S <br />
	**[[3qv6]] – LmPyK + acid blue 80<br />		**[[3qv6]] – LmPyK + acid blue 80<br />
	**[[3e0v]] – LmPyK + sulfate<br />		**[[3e0v]] – LmPyK + sulfate<br />
Line 78:		Line 95:
	**[[3is4]], [[3ktx]] – LmPyK + pyrenetetrasulfonic acid<br />		**[[3is4]], [[3ktx]] – LmPyK + pyrenetetrasulfonic acid<br />
	**[[3t07]] – SaPyK + bis-indole alkaloid<br />		**[[3t07]] – SaPyK + bis-indole alkaloid<br />
	**[[4b2d]] - hPyK M1/M2 + fructose bisphosphate<br />
	**[[4rpp]] - hPyK M2 (mutant) + fructose bisphosphate<br />
	**[[4fxj]] - hPyK M1/M2 + phenylalanine<br />
	**[[6gg4]] - hPyK M2 + phenylalanine<br />
	**[[6gg5]] - hPyK M2 + tryptophan<br />
	**[[6gg6]] - hPyK M2 + serine<br />
	**[[5x1v]], [[5x1w]] - hPyK M2 + inhibitor<br />
	**[[4rpp]] - hPyK M2 (mutant) + fructose bisphosphate<br />
	**[[4hyw]] – TbPyK + fructose bisphosphate – ''Trypanosoma brucei''<br />		**[[4hyw]] – TbPyK + fructose bisphosphate – ''Trypanosoma brucei''<br />
	**[[5ws8]] - MtPyK + oxalate<br />		**[[5ws8]] - MtPyK + oxalate<br />
			**[[6p0y]] - CpPyK + ADP<br />

	*Pyruvate kinase higher complex		*Pyruvate kinase higher complex

	**[[3hqo]] – LmPyK + ATP + oxalate<br />
	**[[3hqp]] - LmPyK + ATP + oxalate + fructose bisphosphate<br />
	**[[3qv7]] – LmPyK + acid blue 25 + Ponceau S<br />
	**[[3srk]] – LmPyK + saccharine + inhibitor<br />
	**[[3n25]] – rPyK M1/M2 + proline + Mn + pyruvate<br />
	**[[2g50]] - rPyK M1/M2 + alanine + Mn + pyruvate<br />
	**[[1pkn]] - rPyK + Mn + pyruvate<br />
	**[[1aqf]] – rPyK + Mg + phospholactate<br />
	**[[1a49]], [[1a5u]] - rPyK + ATP + oxalate<br />
	**[[3me3]] – hPyK M1/M2 + aniline derivative + fructose bisphosphate<br />		**[[3me3]] – hPyK M1/M2 + aniline derivative + fructose bisphosphate<br />
	**[[4g1n]] - hPyK M1/M2 + pyridazine derivative + oxalate<br />		**[[4g1n]] - hPyK M1/M2 + pyridazine derivative + oxalate<br />
Line 110:		Line 111:
	**[[4fxf]] - hPyK M1/M2 + oxalate + ATP + fructose bisphosphate<br />		**[[4fxf]] - hPyK M1/M2 + oxalate + ATP + fructose bisphosphate<br />
	**[[4ima]], [[4ip7]] - hPyK L (mutant) + citrate + adenosine + fructose bisphosphate<br />		**[[4ima]], [[4ip7]] - hPyK L (mutant) + citrate + adenosine + fructose bisphosphate<br />
			**[[3n25]] – rPyK M1/M2 + proline + Mn + pyruvate<br />
			**[[2g50]] - rPyK M1/M2 + alanine + Mn + pyruvate<br />
			**[[1pkn]] - rPyK + Mn + pyruvate<br />
			**[[1aqf]] – rPyK + Mg + phospholactate<br />
			**[[1a49]], [[1a5u]] - rPyK + ATP + oxalate<br />
	**[[1a3w]] – yPyK + Mn + phosphoglycolic acid + fructose bisphosphate – yeast<br />		**[[1a3w]] – yPyK + Mn + phosphoglycolic acid + fructose bisphosphate – yeast<br />
	**[[1a3x]] - yPyK + Mn + phosphoglycolic acid<br />		**[[1a3x]] - yPyK + Mn + phosphoglycolic acid<br />
Line 121:		Line 127:
	**[[5wsa]] – MtPyK + oxalate + glucose-6-phosphate <br />		**[[5wsa]] – MtPyK + oxalate + glucose-6-phosphate <br />
	**[[5wsb]], [[5wsc]] – MtPyK + oxalate + glucose-6-phosphate + AMP<br />		**[[5wsb]], [[5wsc]] – MtPyK + oxalate + glucose-6-phosphate + AMP<br />
			**[[6ito]] – MtPyK + oxalate + ribose-5-phosphate + AMP<br />
			**[[3hqo]] – LmPyK + ATP + oxalate<br />
			**[[3hqp]] - LmPyK + ATP + oxalate + fructose bisphosphate<br />
			**[[3qv7]] – LmPyK + acid blue 25 + Ponceau S<br />
			**[[3srk]] – LmPyK + saccharine + inhibitor<br />
			**[[6qxl]] – PyK + malonate + glucose-6-phosphate + Mg – ''Pseudomonas aerugnosa''<br />

	}}		}}

Michal Harel at 10:09, 30 August 2018

2018-08-30T10:09:56Z

← Older revision		Revision as of 10:09, 30 August 2018
Line 5:		Line 5:
	This particular protein is found in Homo sapiens and has the abbreviation PK. Pyruvate kinase belongs to the all beta proteins class and has the PK beta-barrel domain-like fold. It belongs to the PK beta-barrel domain-like superfamily and pyruvate kinase beta-barrel domain family<ref>{{website\| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]\|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html\|}}</ref>.		This particular protein is found in Homo sapiens and has the abbreviation PK. Pyruvate kinase belongs to the all beta proteins class and has the PK beta-barrel domain-like fold. It belongs to the PK beta-barrel domain-like superfamily and pyruvate kinase beta-barrel domain family<ref>{{website\| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]\|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html\|}}</ref>.

	Though pyruvate kinase is classified into all beta proteins, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of both alpha helices and beta sheets. In the quaternary structure of pyruvate kinase, it can be observed to have <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the <scene name='Keegan_Gelvoria_Sandbox_1/Ligands/1'>K+</scene> and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: L (liver), R (red blood cells), M1 (muscle, heart, and brain), and M2 (early fetal tissue)<ref>{{website\| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]\|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html\|}}</ref>.		Though pyruvate kinase is classified into all beta proteins, pyruvate kinase's <scene name='Keegan_Gelvoria_Sandbox_1/Secondary_structure/1'>secondary structure</scene> comprises of both alpha helices and beta sheets. In the quaternary structure of pyruvate kinase, it can be observed to have <scene name='Keegan_Gelvoria_Sandbox_1/Structure_4_domains/1'>four domains</scene> in humans. Thus, this enzyme is tetrameric with <scene name='Keegan_Gelvoria_Sandbox_1/Metal_binding_sites/1'>metal binding sites</scene> on each domain for the <scene name='Keegan_Gelvoria_Sandbox_1/Ligands/1'>K+</scene> and Mg2+ ligands to bind to. There are four types of tissue-specific isozymes: '''L''' (liver), '''R''' (red blood cells), '''M1''' (muscle, heart, and brain), and '''M2''' (early fetal tissue)<ref>{{website\| title=SCOP: Protein: Pyruvate kinase (PK) from Human (Homo sapiens) [TaxId: 9606]\|url=http://scop.berkeley.edu/data/scop.b.c.jh.b.b.d.html\|}}</ref>.

	==Mechanism==		==Mechanism==
Line 52:		Line 52:
	**[[3khd]] – PyK – ''Plasmodium falciparum''<br />		**[[3khd]] – PyK – ''Plasmodium falciparum''<br />
	**[[3gg8]], [[3eoe]] – PyK – ''Toxoplasma gondii''<br />		**[[3gg8]], [[3eoe]] – PyK – ''Toxoplasma gondii''<br />
	**[[3bjf]], [[3bjt]], [[1t5a]], [[1zjh]] - hPyK M2 - human<br />		**[[3bjf]], [[3bjt]], [[1t5a]], [[1zjh]], [[3srf]], [[3srh]] - hPyK M1/M2 - human<br />
	**[[4wj8]], [[4qg6]], [[4qg8]], [[4qg9]], [[4qgc]], [[3g2g]], [[4yj5]] - hPyK M2 (mutant)<br />		**[[4wj8]], [[4qg6]], [[4qg8]], [[4qg9]], [[4qgc]], [[3g2g]], [[4yj5]] - hPyK M1/M2 (mutant)<br />
	**[[2vgb~~]], [[3srf]], [[3srh~~]] – hPyK<br />		**[[2vgb]] – hPyK R/L<br />
	**[[2vgf]], [[2vgg]], [[2vgi~~]], [[4qg6]], [[4qg8]], [[4qg9]], [[4qgc~~]] - hPyK (mutant) <br />		**[[2vgf]], [[2vgg]], [[2vgi]] - hPyK R/L (mutant) <br />
	**[[3ma8]], [[4drs]] – PyK – ''Cryptosporidium parvum''<br />		**[[3ma8]], [[4drs]] – PyK – ''Cryptosporidium parvum''<br />
	**[[2e28]] - PyK (mutant) – ''Geobacillus stearothermophilus''<br />		**[[2e28]] - PyK (mutant) – ''Geobacillus stearothermophilus''<br />
	**[[1f3w]] – rPyK – rabbit<br />		**[[1f3w]] – rPyK – rabbit<br />
	**[[1f3x]] - rPyK (mutant) <br />		**[[1f3x]] - rPyK (mutant) <br />
	**[[~~1e0t~~]], [[~~1e0u~~]] - ~~EcPyK (mutant) –~~ ''Eschericia coli''<br />		**[[1pky]], [[4yng]] – EcPyK - ''Eschericia coli''<br />
	**[[~~1pky~~]], [[~~4yng~~]] – EcPyK<br />		**[[1e0t]], [[1e0u]] - EcPyK (mutant) <br />
	**[[1pkm]], [[1pyk]] – PyK – cat<br />		**[[1pkm]], [[1pyk]] – PyK – cat<br />
	**[[3t05]], [[3t0t]] – SaPyK – ''Staphylococcus aureus''<br />		**[[3t05]], [[3t0t]] – SaPyK – ''Staphylococcus aureus''<br />
	**[[3qtg]] – PyK – ''Pyrobaculum aerophilum''<br />		**[[3qtg]] – PyK – ''Pyrobaculum aerophilum''<br />
	**[[4krz]] - TcPyK – ''Trypanosoma cruzei''<br />		**[[4krz]] - TcPyK – ''Trypanosoma cruzei''<br />
			**[[5wrp]] - MtPyK – ''Mycobacterium tuberculosis''<br />

	*Pyruvate kinase binary complex		*Pyruvate kinase binary complex
Line 77:		Line 78:
	**[[3is4]], [[3ktx]] – LmPyK + pyrenetetrasulfonic acid<br />		**[[3is4]], [[3ktx]] – LmPyK + pyrenetetrasulfonic acid<br />
	**[[3t07]] – SaPyK + bis-indole alkaloid<br />		**[[3t07]] – SaPyK + bis-indole alkaloid<br />
	**[[4b2d]] - hPyK + fructose bisphosphate<br />		**[[4b2d]] - hPyK M1/M2 + fructose bisphosphate<br />
	**[[4rpp]] - hPyK (mutant) + fructose bisphosphate<br />		**[[4rpp]] - hPyK M2 (mutant) + fructose bisphosphate<br />
	**[[4fxj]] - hPyK + phenylalanine<br />		**[[4fxj]] - hPyK M1/M2 + phenylalanine<br />
			**[[6gg4]] - hPyK M2 + phenylalanine<br />
			**[[6gg5]] - hPyK M2 + tryptophan<br />
			**[[6gg6]] - hPyK M2 + serine<br />
	**[[5x1v]], [[5x1w]] - hPyK M2 + inhibitor<br />		**[[5x1v]], [[5x1w]] - hPyK M2 + inhibitor<br />
	**[[4rpp]] - hPyK M2 (mutant) + fructose bisphosphate<br />		**[[4rpp]] - hPyK M2 (mutant) + fructose bisphosphate<br />
	**[[4hyw]] – TbPyK + fructose bisphosphate – ''Trypanosoma brucei''<br />		**[[4hyw]] – TbPyK + fructose bisphosphate – ''Trypanosoma brucei''<br />
			**[[5ws8]] - MtPyK + oxalate<br />

	*Pyruvate kinase ~~ternary~~ complex		*Pyruvate kinase higher complex

	**[[3hqo]] – LmPyK + ATP + oxalate<br />		**[[3hqo]] – LmPyK + ATP + oxalate<br />
Line 90:		Line 95:
	**[[3qv7]] – LmPyK + acid blue 25 + Ponceau S<br />		**[[3qv7]] – LmPyK + acid blue 25 + Ponceau S<br />
	**[[3srk]] – LmPyK + saccharine + inhibitor<br />		**[[3srk]] – LmPyK + saccharine + inhibitor<br />
	**[[3n25]] – rPyK + proline + Mn + pyruvate<br />		**[[3n25]] – rPyK M1/M2 + proline + Mn + pyruvate<br />
	**[[2g50]] - rPyK + alanine + Mn + pyruvate<br />		**[[2g50]] - rPyK M1/M2 + alanine + Mn + pyruvate<br />
	**[[1pkn]] - rPyK + Mn + pyruvate<br />		**[[1pkn]] - rPyK + Mn + pyruvate<br />
	**[[1aqf]] – rPyK + Mg + phospholactate<br />		**[[1aqf]] – rPyK + Mg + phospholactate<br />
	**[[1a49]], [[1a5u]] - rPyK + ATP + oxalate<br />		**[[1a49]], [[1a5u]] - rPyK + ATP + oxalate<br />
	**[[3me3]] – hPyK M2 + aniline derivative + fructose bisphosphate<br />		**[[3me3]] – hPyK M1/M2 + aniline derivative + fructose bisphosphate<br />
	**[[4g1n]] - hPyK M2 + pyridazine derivative + oxalate<br />		**[[4g1n]] - hPyK M1/M2 + pyridazine derivative + oxalate<br />
	**[[3h6o]] - hPyK M2 + pyridazine derivative + fructose bisphosphate<br />		**[[3h6o]] - hPyK M1/M2 + pyridazine derivative + fructose bisphosphate<br />
	**[[3gqy]], [[3gr4]], [[3u2z]] - hPyK M2 + piperazine derivative + fructose bisphosphate<br />		**[[3gqy]], [[3gr4]], [[3u2z]] - hPyK M1/M2 + piperazine derivative + fructose bisphosphate<br />
	**[[4jpg]] - hPyK M2 + pyrimidine derivative + fructose bisphosphate<br />		**[[5x0i]] - hPyK M2 (mutant) + serine + fructose bisphosphate<br />
	**[[3srd]] - hPyK + oxalate + fructose bisphosphate<br />		**[[5x1v]], [[5x1w]] - hPyK M2 + activator + fructose bisphosphate<br />
	**[[4fxf]] - hPyK + oxalate + ATP + fructose bisphosphate<br />		**[[4jpg]] - hPyK M1/M2 + pyrimidine derivative + fructose bisphosphate<br />
	**[[4ima]], [[4ip7]] - hPyK (mutant) + citrate + adenosine + fructose bisphosphate<br />		**[[3srd]] - hPyK M1/M2 + oxalate + fructose bisphosphate<br />
			**[[4fxf]] - hPyK M1/M2 + oxalate + ATP + fructose bisphosphate<br />
			**[[4ima]], [[4ip7]] - hPyK L (mutant) + citrate + adenosine + fructose bisphosphate<br />
	**[[1a3w]] – yPyK + Mn + phosphoglycolic acid + fructose bisphosphate – yeast<br />		**[[1a3w]] – yPyK + Mn + phosphoglycolic acid + fructose bisphosphate – yeast<br />
	**[[1a3x]] - yPyK + Mn + phosphoglycolic acid<br />		**[[1a3x]] - yPyK + Mn + phosphoglycolic acid<br />
Line 111:		Line 118:
	**[[4kcw]] – TbPyK + oxalate + fructose bisphosphate <br />		**[[4kcw]] – TbPyK + oxalate + fructose bisphosphate <br />
	**[[4ks0]] – TcPyK + oxalate + fructose bisphosphate <br />		**[[4ks0]] – TcPyK + oxalate + fructose bisphosphate <br />
			**[[5ws9]] – MtPyK + oxalate + AMP + ATP <br />
			**[[5wsa]] – MtPyK + oxalate + glucose-6-phosphate <br />
			**[[5wsb]], [[5wsc]] – MtPyK + oxalate + glucose-6-phosphate + AMP<br />

	}}		}}

Alexander Berchansky at 11:26, 4 June 2018

2018-06-04T11:26:25Z

← Older revision		Revision as of 11:26, 4 June 2018
Line 8:		Line 8:

	==Mechanism==		==Mechanism==
	[[Image:Pyruvatekinasemechanism.gif\| left \| ~~thumb \| 880px~~]]		[[Image:Pyruvatekinasemechanism.gif\| left \| 500px]]
	<ref>{{website1\| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?\|url=http://www.sportsci.org/jour/0102/rar.htm\|}}</ref>		<ref>{{website1\| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?\|url=http://www.sportsci.org/jour/0102/rar.htm\|}}</ref>
	<scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates one K+ and two Mg2+ cations to be used in two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=502\|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=503\|}}</ref>.		<scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates one K+ and two Mg2+ cations to be used in two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=502\|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=503\|}}</ref>.

Alexander Berchansky at 11:25, 4 June 2018

2018-06-04T11:25:57Z

← Older revision		Revision as of 11:25, 4 June 2018
Line 8:		Line 8:

	==Mechanism==		==Mechanism==
	[[Image:Pyruvatekinasemechanism.gif\| left \| thumb \| ]]		[[Image:Pyruvatekinasemechanism.gif\| left \| thumb \| 880px]]
	<ref>{{website1\| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?\|url=http://www.sportsci.org/jour/0102/rar.htm\|}}</ref>		<ref>{{website1\| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?\|url=http://www.sportsci.org/jour/0102/rar.htm\|}}</ref>
	<scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates one K+ and two Mg2+ cations to be used in two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=502\|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=503\|}}</ref>.		<scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates one K+ and two Mg2+ cations to be used in two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=502\|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=503\|}}</ref>.

Alexander Berchansky at 11:25, 4 June 2018

2018-06-04T11:25:34Z

← Older revision		Revision as of 11:25, 4 June 2018
Line 8:		Line 8:

	==Mechanism==		==Mechanism==
	[[Image:Pyruvatekinasemechanism.gif\| left \| thumb \| ~~600px~~]]		[[Image:Pyruvatekinasemechanism.gif\| left \| thumb \| ]]
	<ref>{{website1\| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?\|url=http://www.sportsci.org/jour/0102/rar.htm\|}}</ref>		<ref>{{website1\| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?\|url=http://www.sportsci.org/jour/0102/rar.htm\|}}</ref>
	<scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates one K+ and two Mg2+ cations to be used in two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=502\|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=503\|}}</ref>.		<scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates one K+ and two Mg2+ cations to be used in two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=502\|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=503\|}}</ref>.

Alexander Berchansky at 11:25, 4 June 2018

2018-06-04T11:25:14Z

← Older revision		Revision as of 11:25, 4 June 2018
Line 8:		Line 8:

	==Mechanism==		==Mechanism==
	[[Image:Pyruvatekinasemechanism.gif\| left \| thumb \| ~~550px~~]]		[[Image:Pyruvatekinasemechanism.gif\| left \| thumb \| 600px]]
	<ref>{{website1\| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?\|url=http://www.sportsci.org/jour/0102/rar.htm\|}}</ref>		<ref>{{website1\| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?\|url=http://www.sportsci.org/jour/0102/rar.htm\|}}</ref>
	<scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates one K+ and two Mg2+ cations to be used in two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=502\|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=503\|}}</ref>.		<scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates one K+ and two Mg2+ cations to be used in two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=502\|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=503\|}}</ref>.

Alexander Berchansky at 11:24, 4 June 2018

2018-06-04T11:24:45Z

← Older revision		Revision as of 11:24, 4 June 2018
Line 8:		Line 8:

	==Mechanism==		==Mechanism==
	[[Image:Pyruvatekinasemechanism.gif\|left\|thumb\|~~500px~~]]		[[Image:Pyruvatekinasemechanism.gif\| left \| thumb \| 550px]]
	<ref>{{website1\| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?\|url=http://www.sportsci.org/jour/0102/rar.htm\|}}</ref>		<ref>{{website1\| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?\|url=http://www.sportsci.org/jour/0102/rar.htm\|}}</ref>
	<scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates one K+ and two Mg2+ cations to be used in two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=502\|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=503\|}}</ref>.		<scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates one K+ and two Mg2+ cations to be used in two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=502\|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=503\|}}</ref>.

Alexander Berchansky at 11:23, 4 June 2018

2018-06-04T11:23:06Z

← Older revision		Revision as of 11:23, 4 June 2018
Line 8:		Line 8:

	==Mechanism==		==Mechanism==
	[[Image:Pyruvatekinasemechanism.gif\|left\|thumb\|~~450px~~]]		[[Image:Pyruvatekinasemechanism.gif\|left\|thumb\|500px]]
	<ref>{{website1\| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?\|url=http://www.sportsci.org/jour/0102/rar.htm\|}}</ref>		<ref>{{website1\| title=Exercise-Induced Metabolic Acidosis: Where do the Protons come from?\|url=http://www.sportsci.org/jour/0102/rar.htm\|}}</ref>
	<scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates one K+ and two Mg2+ cations to be used in two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=502\|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=503\|}}</ref>.		<scene name='Keegan_Gelvoria_Sandbox_1/N_c_rainbow/null'>Pyruvate Kinase</scene> catalyzes the final reaction of glycolysis. It couples the free energy of PEP cleavage to the generation of ATP during the synthesis of the final product, pyruvate. This reaction necessitates one K+ and two Mg2+ cations to be used in two steps. The first step is the nucleophilic attack of the PEP phosphorous atom by β-phosphoryl oxygen of ADP; this step displaces enolpyruvate while forming ATP. In the second step, enolpyruvate tautomerizes to pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=502\|}}</ref>. The formation of a high-energy intermediate by enolase in the 9th reaction of glycolysis allows for the synthesis of ATP in this reaction. Though the hydrolysis of 2PG is insufficient in driving the synthesis of ATP, the dehydration of 2PG allows for such a reaction to occur by forming a high-energy intermediate. The high potential of PEP reflects the large release of energy that occurs with the conversion of enolpyruvate to its keto tautomer, pyruvate <ref>{{book \|author=Voet, Donald; Voet, Judith C.; Pratt, Charlotte W.\|title=Fundamentals of Biochemistry: Life at the Molecular Level\|edition= 3\|pages=503\|}}</ref>.