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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1agy

E.C. namecutinase
SpeciesFusarium solani subsp. pisi (Nectria haematococca)
E.C. Number (IntEnz) 3.1.1.74
CSA Homologues of 1agyThere are 47 Homologs
CSA Entries With UniProtID P00590
CSA Entries With EC Number 3.1.1.74
PDBe Entry 1agy
PDBSum Entry 1agy
MACiE Entry 1agy

Literature Report

IntroductionCutinase is a serine esterase. It hydrolyses cutin, an insoluble polyester which covers the surface of plants. It is also able to hydrolyse fatty acids esters and emulsified triacylglycerol as efficiently as lipases.
MechansimHis188 acts as a base to deprotonate Ser120 to allow its nucleophilic attack on the ester bond. His188 donates a proton to the leaving group and then activates a water molecule to allow the hydrolysis of the acylenzyme. Asp175 alters the pKa of the His188 to allow to act as an effective base in the reaction. Gln121 and Ser42 forms the oxyanion hole to stabilise the transition state.
Reaction

Catalytic Sites for 1agy

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AspA175191macie:sideChainIt alters the pKa of His 188 to allow it to act as an effective acid/base in the reaction.
GlnA121137macie:sideChainIt forms the oxyanion hole to stabilise the transition state.
SerA4258macie:mainChainAmideIt forms the oxyanion hole, stabilising the tetrahedral transition state.
SerA120136macie:sideChainIt acts as a nucleophile to attack the ester bond.
HisA188204macie:sideChainIt deprotonates Ser 120 to allow its nucleophilic attack on the ester bond. It donates a proton to the leaving group. It activates a water molecule to promote the hydrolysis of the acylenzyme intermediate.

Literature References

Notes:
Martinez C
Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent.
Nature 1992 356 615-618
PubMed: 1560844
Martinez C
Cutinase, a lipolytic enzyme with a preformed oxyanion hole.
Biochemistry 1994 33 83-89
PubMed: 8286366
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