Lipase: Difference between revisions

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*  The '''bile salt-stimulated lipase''' (BSSL) is found in breast milk.<br />
*  The '''bile salt-stimulated lipase''' (BSSL) is found in breast milk.<br />
*  The '''hormone-sensitive lipase''' (LIPE) hydrolyzes a variety of esters.  For details see [[Hormone sensitive lipase]].<br />
*  The '''hormone-sensitive lipase''' (LIPE) hydrolyzes a variety of esters.  For details see [[Hormone sensitive lipase]].<br />
*  '''Monoacylglycerol lipase''' (MAGL) hydrolyzes intracellular triglycerides to fatty acid and glycerol.  MAGL functions together with LIPE.  For details see [[Monoglyceride lipase]].br/>
*  '''Monoacylglycerol lipase''' (MAGL) hydrolyzes intracellular triglycerides to fatty acid and glycerol.  MAGL functions together with LIPE.  For details see [[Monoglyceride lipase]].


The reaction catalyzed by the enzyme is shown below.  
The reaction catalyzed by the enzyme is shown below.  
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[[Image:Picture 1.png]]   
[[Image:Picture 1.png]]   
Further breakdown ultimately results in 2-monoacylglycerols and free fatty acids <ref name= "A cross-linked complex between horse pancreatic lipase and colipase">[http://www.sciencedirect.com/science/article/pii/0014579389815923] A cross-linked complex between horse pancreatic lipase and colipase</ref>. An in depth discussion of the mechanism can be found in the Lipase Catalytic Mechanism section. The determination of the structure and function of lipase was a gradual process.  Lipase activity was first demonstrated in the pancreas by Claude Bernard in 1846.  However, it wasn't until 1955 that Mattson and Beck demonstrated a high-specificity of pancreatic lipase for triglyceride primary esters <ref name= "History of Lipids">[http://www.cyberlipid.org/history/history1.htm] History of Lipids</ref>.  In recent years, determination of the crystal structure of pancreatic lipase has become the primary focus as many scientists have worked to further this.<br />
Further breakdown ultimately results in 2-monoacylglycerols and free fatty acids <ref name= "A cross-linked complex between horse pancreatic lipase and colipase">[http://www.sciencedirect.com/science/article/pii/0014579389815923] A cross-linked complex between horse pancreatic lipase and colipase</ref>. An in depth discussion of the mechanism can be found in the Lipase Catalytic Mechanism section. The determination of the structure and function of lipase was a gradual process.  Lipase activity was first demonstrated in the pancreas by Claude Bernard in 1846.  However, it wasn't until 1955 that Mattson and Beck demonstrated a high-specificity of pancreatic lipase for triglyceride primary esters <ref name= "History of Lipids">[http://www.cyberlipid.org/history/history1.htm] History of Lipids</ref>.  In recent years, determination of the crystal structure of pancreatic lipase has become the primary focus as many scientists have worked to further this.<br />
=='''See also'''==<br />
 
==See also==
* [[Molecular Playground/Pancreatic Lipase]]<br />
* [[Molecular Playground/Pancreatic Lipase]]<br />
* [[Lipase lid morph]]<br />
* [[Lipase lid morph]]<br />
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* [[Monoglyceride lipase]]<br />
* [[Monoglyceride lipase]]<br />
* [[Human gastric lipase]]<br />
* [[Human gastric lipase]]<br />
* [[Lipoprotein Lipase (LPL) complexed with GPIHBP1]]<br />
* [[Lipase (Hebrew)]]<br />
* [[Lipase (Hebrew)]]<br />
* [[Lipid metabolism]]


== '''Structure''' ==
== '''Structure''' ==
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</StructureSection>
</StructureSection>


== 3D Structures of Lipase ==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|
*Eukaryote lipase:
**[[1hpl]] – hLip – horse <br />
**[[1hlg]] – hLip – human - gastric<br />
**[[1jmy]] – hBSSL  <br />
**[[1akn]] – cBSSL – cattle <br />
**[[2bce]] - cBSSL (mutant) <br />
**[[1f6w]] - cBSSL – catalytic domain<br />
**[[3o0d]] – Lip – ''Yarrowia lipolytica''<br />
**[[4jei]] – YlLip (mutant)<br />
**[[1gpl]] – Lip – Guinea pig<br />
**[[3zpx]] – Lip – ''Ustilago maydis''<br />
**[[6a0w]] – Lip catalytic domain – bread mold<br />
**[[4zrd]], [[4zre]] – Lip1 (mutant) – dandruff fungus<br />
*Prokaryote lipase:
**[[1llf]] – Lip – ''Candida cylindracea''<br />
**[[3g7n]] – Lip - ''Penicillium expansum''<br />
**[[1tia]] - Lip – ''Penicillium camemberti''<br />
**[[2hih]] – Lip – ''Staphylococcus hyicus''<br />
**[[2fx5]] – Lip – ''Pseudomonas mendocina''<br />
**[[1yzf]] – Lip – ''Enterococcus faecalis''<br />
**[[1dt3]], [[1dt5]], [[1dte]], [[1du4]], [[1ein]], [[1tib]], [[4dyh]], [[4ea6]], [[4flf]], [[4gbg]], [[4gwl]], [[4zgb]], [[6hw1]] - TlLip - ''Thermomyces lanuginose''<br />
**[[5ap9]] – TlLip (mutant)<br />
**[[1jfr]] – Lip – ''Streptomyces exfoliates''<br />
**[[5mal]] – Lip – ''Streptomyces rimosus''<br />
**[[2lip]] – BcLip – open state<br />
**[[1cvl]] – Lip – ''Chromobacterium viscosum''<br />
**[[1tic]] - Lip  – ''Rhizopus oryzae''<br />
**[[3tgl]], [[4tgl]], [[1tgl]], [[6qpp]] – RmLip – ''Rhyzomucor miehei''<br />
**[[6qpr]] – RmLip (mutant)<br />
**[[2zvd]] – PsLip - ''Pseudomonas sp.'' – open state<br />
**[[2z8x]] - PsLip – extracellular<br />
**[[5xpx]] – PsLip residues 1-388<br />
**[[2zj6]], [[2zj7]] – PsLip (mutant) <br />
**[[2z8z]] – PsLip(mutant) – closed state<br />
**[[3lip]], [[3a6z]] - Lip - ''Pseudomonas cepacia'' – open state<br />
**[[1qge]], [[1tah]] – Lip – ''Pseudomonas glumae''<br />
**[[2w22]], [[6a12]] – GtLip – ''Geobacillus thermocatenulatus''<br />
**[[5ce5]] – GtLip (mutant)<br />
**[[1ji3]], [[1ku0]], [[4fmp]], [[4x6u]] – BstLip – ''Bacillus stearothermophilus''<br />
**[[4x71]], [[4x7b]], [[4x85]], [[6s3g]], [[6s3j]], [[6s3v]], [[6fz1]], [[6fz7]], [[6fz8]], [[6fz9]], [[6fza]], [[6fzc]], [[6fzd]] – BstLip (mutant)<br />
**[[1ah7]] - Lip – ''Bacillus cereus''<br />
**[[2ory]] – Lip – ''Photobacterium lypoliticum''<br />
**[[2z5g]], [[2dsn]] – GzLip T1 – ''Geobacillus zalihae''<br />
**[[3umj]] – GzLip (mutant)<br />
**[[3p94]] – Lip – ''Parabacteroides distasonis''<br />
**[[3ngm]] – Lip – ''Gibberella zeae''<br />
**[[3auk]] - Lip – ''Geobacillus''<br />
**[[3uue]], [[3uuf]] – Lip – ''Malassezia globosa''<br />
**[[4hs9]] – Lip – ''Proteus mirabilis''<br />
**[[4opm]] – Lip – ''Acinetobacter baumannii''<br />
**[[5ah0]] – Lip – ''Pelosinus fermentans''<br />
**[[5ah1]] – Lip – ''Clostridium botulinum''<br />
**[[5ch8]] – Lip (mutant) – ''Penicillium cyclopium''<br />
*Bacterial lipase A
**[[3guu]] – CaLipA – ''Candida Antarctica''<br />
**[[2veo]] – CaLipA – closed state<br />
**[[2qua]], [[2qub]] – SmLipA – ''Serratia marcescens''<br />
**[[2qxt]], [[2qxu]], [[1isp]], [[1i6w]], [[5ct4]], [[5ct5]], [[5ct6]], [[5cri]] - BsLipA  – ''Bacillus subtilis''<br />
**[[3d2a]], [[3d2b]], [[3d2c]], [[1t2n]], [[1t4m]], [[5ct8]], [[5ct9]], [[5cta]], [[5cur]], [[3qzu]], [[3qmm]] - BsLipA (mutant) <br />
**[[1r4z]] – BsLipA+Rc-IPG-phosphonate<br />
**[[1r50]] – BsLipA +Sc-IPG-phosphonate<br />
*Bacterial lipase B
**[[4zv7]], [[3w9b]], [[5a6v]], [[5a71]], [[4k6g]], [[1tca]], [[1tcb]], [[1tcc]], [[1lbs]], [[1lbt]] – CaLipB <br />
**[[3icv]], [[4k5q]], [[5k6h]], [[5k6k]] – CaLipB (mutant) <br />
**[[5gv5]] - CaLipB + phosphonate<br />
**[[3icw]] – CaLipB (mutant) + phosphonate<br />
**[[5x7k]] – SmLipB NBD <br />
**[[6isp]], [[6isq]], [[6isr]] – LipB (mutant) – ''Pseudozyma antarctica''<br />
**[[6idy]] - AfLipB -  ''Aspergillus fumigatus''<br />
*Bacterial lipase C
**[[5nen]] – SmLipC residues 1-443 <br />
*Lipase/colipase complexes.  The colipase is a co-enzyme whose binding to lipase optimizes the enzymatic activity
**[[1n8s]] – hLip+colipase II<br />
**[[1eth]], [[1lpa]] - pLip+colipase II - pig<br />
*Hormone-sensitive-lipases (LIPE) hydrolyze the first fatty acid of the triacylglycerol substrate
**[[3k6k]] – EstE7(LIPE) – metagenome library<br />
**[[3fak]], [[3dnm]] – EstE5(LIPE) – metagenome library<br />
**[[1evq]] – AaEst2(LIPE) – ''Alicyclobacillus acidocaldarius''<br />
**[[1u4n]] – AaEst2(LIPE) (mutant) <br />
*Putative lipases; Proteins with unknown function but structural similarity to lipase obtained in structural genomics projects.
**[[2rau]] - Lip – ''Sulfolobus solfataricus''<br />
**[[3bxp]], [[3d3n]] - Lip – ''Lactobacillus plantarum''<br />
**[[3e0x]] - Lip – ''Clostridium acetobutylicum''<br />
**[[1z8h]] – Lip – ''Nostoc sp.'' PCC 712<br />
**[[1vj3]] - Lip  – ''Nostoc sp.'' <br />
**[[3bzw]] – Lip - ''Bacteroides thetaiotaomicron''<br />
**[[2pbl]] – Lip - ''Silicibacter''
*Lipase + inhibitors
**[[3l1h]] – EstE5(LIPE)+FeCl3  – noninvasive inhibitor<br />
**[[3l1i]], [[3l1j]] - EstE5(LIPE)+CuSO4 – noninvasive inhibitor<br />
**[[3lij]] - EstE5(LIPE)+ZnSO4– noninvasive inhibitor<br />
**[[3h18]], [[3h17]] - EstE5 (LIPE)+PMSF <br />
**[[3h19]], [[3h1b]], [[3h1a]] – EstE5 (LIPE)+methyl alcohol<br />
**[[3h1a]] – EstE5 SLIPE)+ethyl alcohol<br />
**[[3h19]] – EstE5 SLIPE)+isopropyl alcohol<br />
**[[3g9t]], [[3g9u]] - EstE5 (HSLIPE)+p-nitrophenyl butyrate<br />
**[[3g9z]] - EstE5 (LIPE) +p-nitrophenyl caprylate<br />
**[[2nw6]] – BcLip+ S inhibitor <br />
**[[4lip]], [[5lip]], [[1r4z]], [[1r50]] – BcLip+ Rc-(Rp,Sp)-1,2-dioctylcarbamoyl-glycero-3-O-phosphonate<br />
**[[1k8q]] - Lip+phosphonate – dog <br />
**[[1ex9]] – Lip+Rc-(Rp,Sp)-1,2-dioctylcarbamoyl-glycero-3-O-phosphonate – ''Pseudomonas aeruginosa'' <br />
**[[5tgl]] – RmLip+N-hexyl-phosphonate <br />
**[[1lpb]] – pLip + colipase+C11 alkyl phosphonate <br />
**[[3a70]] – PsLip+diethyl phosphate<br />
**[[4glb]] – TlLip + nitrobenzaldehyde<br />
**[[4kjx]] - TlLip + nitrobenzaldehyde + lauric acid<br />
**[[4n8s]] - TlLip + nitrobenzaldehyde + ethylacetoacetate<br />
**[[4s0x]] – TlLip + lauric acid<br />
*Lipase conjugated with analogs to its reaction intermediates
**[[1qz3]] – EaEst2(mutant) (LIPE)+hexadecanesulfonate <br />
*Bile-salt activated lipase
**[[6h0t]] – hBAL (mutant) <br />
**[[6h0v]], [[6h18]], [[6h19]], [[6h1a]] – hBAL (mutant) + nerve agent<br />
**[[1aql]] – bBAL+taurocholate - bovine<br />
*Monoacylglycerol lipase
**[[3hju]], [[3jw8]] - hMAGL  <BR />
**[[3jwe]], [[3pe6]], [[4uuq]], [[6ax1]], [[6bq0]] – hMAGL + inhibitor<br />
**[[4uuq]] - hMAGLip + SAR <br />
**[[5zun]] – hMAGL (mutant) + inhibitor<br />
**[[3rm3]], [[4lhe]], [[5xks]] - BaMAGL – ''Bacillus'' <BR />
**[[3rli]] – BaMAGL + PMSF<br />
**[[4ke7]], [[4ke8]], [[4ke9]] – BaMAGL + ligand<br />
**[[4ke6]], [[4kea]] – BaMAGL (mutant) + ligand<br />
**[[4zwn]] – yMAGL – yeast<br />
**[[4zxf]] – yMAGLip + substrate analog<br />
**[[6eic]] – MAGLip – ''Mycobacterium tuberculosis''<br />
**[[5xk2]] – MAGLip – ''Aespergillus oryzae''<br />
*Lipase with substrate bound at active site
**[[2zyh]] – AfLip (mutant)+fatty acid – ''Archaeoglobus fulgidus''<br />
**[[2zyi]], [[2zyr]], [[2zys]] - AfLip+fatty acid+ ion <br />
**[[1gt6]], [[4ghw]], [[4gi1]] – TlLip+ fatty acid - lipid ligand<br />
*Lipase conjugated to transition-state analogs showing the binding mode of the enzyme catalysis
**[[1ys1]] – BhLip+hexylphosphonic acid (R) 2-methyl-3-phenylpropyl ester <br />
**[[1ys2]] – BhLip+hexylphosphonic acid (S) 2-methyl-3-phenylpropyl ester<br /> 
**[[1hqd]] – Lip+1-phenoxy-2-acrtoxy butane – ''Pseudomonas cepacia'' <br />
*Lipase+lipase chaperone
**[[2es4]] – Lip+lipase chaperone C-terminal - ''Burkholderia glumae''
*Lipase 2 or esterase/lipase
**[[3v9a]],[[3g9t]], [[3g9u]], [[3g9z]], [[3h19]], [[3h1a]], [[3h1b]], [[3l1h]], [[3l1i]], [[3l1j]], [[3fak]], [[3h17]], [[3h18]], [[3dnm]], [[3k6k]] - E/L -  uncultured bacteria<br />
**[[3w9b]] - CaE/L <br />
**[[4v2i]] - E/L -  ''Thalassospira''<br />
**[[4n5h]] - LrE/L (mutant) -  ''Lactobacillus rhamnosus''<br />
**[[4n5i]] - LrE/L + inhibitor <br />
**[[4ouk]] - LrE/L (mutant) + inhibitor <br />
**[[4bzz]], [[4bzw]] - LpE/L <br />
**[[6gup]] - AfE/L <br />
**[[1lgy]] – Lip2 – ''Rhizopus niveus''<br />
**[[1gz7]] - CrLip2 <br />
**[[4jei]] – Lip2 – ''Yarrowia lipolytica''<br />
**[[1thg]] – Lip2 – ''Geotrichum candidum''<br />
}}
==References==
==References==
<references />
<references />


[[Category:Topic Page]]
[[Category:Topic Page]]