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Catalytic Site Atlas

CSA LITERATURE entry for 1r4z

E.C. nametriacylglycerol lipase
SpeciesBacillus subtilis (Bacteria)
E.C. Number (IntEnz) 3.1.1.3
CSA Homologues of 1r4zThere are 10 Homologs
CSA Entries With UniProtID P37957
CSA Entries With EC Number 3.1.1.3
PDBe Entry 1r4z
PDBSum Entry 1r4z
MACiE Entry 1r4z

Literature Report

IntroductionLipases catalyse the hydrolysis and synthesis of long-chain triglycerols. They have important industrial applications in resolution of racemic mixtures, ester synthesis and transesterification reactions, as well as additives in washing powders.
MechansimHis 156 activates Ser 77 through general base catalysis to deprotonate Ser 77 allowing it to make a nucleophilic attack on the ester bond. His 156 donates a proton to the leaving group and then activates a water molecule to allow the hydrolysis of the acyl-enzyme intermediate, again by general base catalysis. Asp 133 alters the pKa of the His 156 to activate it and allow it to act as an effective base in the reaction. The Ile 12 and Met 78 backbone amides form the oxyanion hole to stabilise the transition state.
Reaction

Catalytic Sites for 1r4z

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AspA133164macie:sideChainAlters the pKa of His 156 to allow it to act as a more efficient general base catalyst.
HisA156187macie:sideChainActs as a general acid/base catalyst to activate Ser 77 and water for nucleophilic attack by proton abstraction, and to facilitate collapse of intermediates and formation of products by proton donation.
MetA78109macie:mainChainAmideStabilises the transition state by formation of the oxyanion hole.
SerA77108macie:sideChainActs as the active site nucleophile in attack of the substrate, to form the acyl-enzyme intermediate.
IleA1243macie:mainChainAmideForms the oxyanion hole to stabilise the transition state.

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AspB133164macie:sideChainAlters the pKa of His 156 to allow it to act as a more efficient general base catalyst.
HisB156187macie:sideChainActs as a general acid/base catalyst to activate Ser 77 and water for nucleophilic attack by proton abstraction, and to facilitate collapse of intermediates and formation of products by proton donation.
MetB78109macie:mainChainAmideStabilises the transition state by formation of the oxyanion hole.
SerB77108macie:sideChainActs as the active site nucleophile in attack of the substrate, to form the acyl-enzyme intermediate.
IleB1243macie:mainChainAmideForms the oxyanion hole to stabilise the transition state.

Literature References

Notes:
van Pouderoyen G
The crystal structure of Bacillus subtilis lipase: a minimal alpha/beta hydrolase fold enzyme.
J Mol Biol 2001 309 215-226
PubMed: 11491291
Kawasaki K
Alternate conformations observed in catalytic serine of Bacillus subtilis lipase determined at 1.3 A resolution.
Acta Crystallogr D Biol Crystallogr 2002 58 1168-1174
PubMed: 12077437
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