Phosphoglycerate Kinase: Difference between revisions

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The general mechanism is a single displacement Sn2 reaction in which the ADP-B-phosphate oxygen atom initiates nucleophilic attack on the 1-phosphate group of 1-3biphosphoglycerate. Thus, the phosphoryl group is transferred directly via a charged transition state. The product, ATP, is favored because it's negatively charged oxygens of the 3 phosphates form <scene name='Shane_Harmon_Sandbox/Atp/3'>hydrogen bonds</scene> with the enzyme. The 3 hydrogen bonds of ATP are favored over the 2 hydrogen bonds of ADP.

The general mechanism is a single displacement Sn2 reaction in which the ADP-B-phosphate oxygen atom initiates nucleophilic attack on the 1-phosphate group of 1-3biphosphoglycerate. Thus, the phosphoryl group is transferred directly via a charged transition state. The product, ATP, is favored because it's negatively charged oxygens of the 3 phosphates form <scene name='Shane_Harmon_Sandbox/Atp/5'>hydrogen bonds</scene> with the enzyme. The 3 hydrogen bonds of ATP are favored over the 2 hydrogen bonds of ADP.

It has been proposed that the transition state intermediary is stabilized by the highly conserved positive Lys 197 as it transfers the phosphate group. Additionally, it has been shown that Arg 38(36) is also necessary for catalytic function. Arg 38(36) has been shown to stabilize a water molecule which is……..

Phosphoglycerate Kinase: Difference between revisions

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Revision as of 23:57, 30 March 2010 view source Shane Harmon (talk \| contribs) 60 edits →Phosphoglycerate Kinase(PGK) ← Older edit		Revision as of 00:51, 31 March 2010 view source Shane Harmon (talk \| contribs) 60 edits →Phosphoglycerate Kinase(PGK) Newer edit →
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	The general mechanism is a single displacement Sn2 reaction in which the ADP-B-phosphate oxygen atom initiates nucleophilic attack on the 1-phosphate group of 1-3biphosphoglycerate. Thus, the phosphoryl group is transferred directly via a charged transition state. The product, ATP, is favored because it's negatively charged oxygens of the 3 phosphates form <scene name='Shane_Harmon_Sandbox/Atp/3'>hydrogen bonds</scene> with the enzyme. The 3 hydrogen bonds of ATP are favored over the 2 hydrogen bonds of ADP.		The general mechanism is a single displacement Sn2 reaction in which the ADP-B-phosphate oxygen atom initiates nucleophilic attack on the 1-phosphate group of 1-3biphosphoglycerate. Thus, the phosphoryl group is transferred directly via a charged transition state. The product, ATP, is favored because it's negatively charged oxygens of the 3 phosphates form <scene name='Shane_Harmon_Sandbox/Atp/5'>hydrogen bonds</scene> with the enzyme. The 3 hydrogen bonds of ATP are favored over the 2 hydrogen bonds of ADP.

	It has been proposed that the transition state intermediary is stabilized by the highly conserved positive Lys 197 as it transfers the phosphate group. Additionally, it has been shown that Arg 38(36) is also necessary for catalytic function. Arg 38(36) has been shown to stabilize a water molecule which is……..		It has been proposed that the transition state intermediary is stabilized by the highly conserved positive Lys 197 as it transfers the phosphate group. Additionally, it has been shown that Arg 38(36) is also necessary for catalytic function. Arg 38(36) has been shown to stabilize a water molecule which is……..