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Catalytic Site Atlas Version 2.2.12
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CSA entry for 1agy
Original Entry
Title:
Serine esterase
Compound:
Cutinase
Mutant:
No
UniProt/Swiss-Prot:
P00590-CUTI_FUSSO
EC Class:
3.1.1.-
Other CSA Entries:
Overview of all sites for 1agy
Homologues of 1agy
Entries for UniProt/Swiss-Prot: P00590
Entries for EC: 3.1.1.-
Other Databases:
PDB entry: 1agy
PDBsum entry: 1agy
UniProt/Swiss-Prot: P00590
IntEnz entry: 3.1.1.-
Literature Report:
Introduction:
Cutinase 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.
Mechanism:
His188 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.
Sites:

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Found by:
Literature reference 

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
SERA 42 58Backbone amide
ElectrostaticTransition state
It forms the oxyanion hole, stabilising the tetrahedral transition state.
Evidence from paper Evidence concerns Evidence type
PubMed ID 8286366 Current protein Residue is positioned appropriately (ligand position known)

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
SERA 120 136Sidechain
NucleophileSubstrate
It acts as a nucleophile to attack the ester bond.
Evidence from paper Evidence concerns Evidence type
PubMed ID 8286366 Current protein Residue is covalently bound to intermediate, based on structural data
PubMed ID 1560844 Current protein Structural similarity to homologue of known mechanism

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
GLNA 121 137Sidechain
ElectrostaticTransition state
It forms the oxyanion hole to stabilise the transition state.
Evidence from paper Evidence concerns Evidence type
PubMed ID 8286366 Current protein Residue is positioned appropriately (ligand position known)

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
ASPA 175 191Sidechain
ElectrostaticResidue
It alters the pKa of His 188 to allow it to act as an effective acid/base in the reaction.
Evidence from paper Evidence concerns Evidence type
PubMed ID 1560844 Current protein Structural similarity to homologue of known mechanism

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
HISA 188 204Sidechain
Acid/baseResidue
Acid/baseWater
It 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.
Evidence from paper Evidence concerns Evidence type
PubMed ID 1560844 Current protein Structural similarity to homologue of known mechanism
References:
1
Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent.
C. Martinez and P. De Geus and M. Lauwereys and G. Matthyssens and C. Cambillau
Nature 356, (6370) 615-8, (1992).
1560844
2
Cutinase, a lipolytic enzyme with a preformed oxyanion hole.
C. Martinez and A. Nicolas and H. van Tilbeurgh and M. P. Egloff and C. Cudrey and R. Verger and C. Cambillau
Biochemistry 33, (1) 83-9, (1994).
8286366
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