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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 9pap

E.C. namepapain
SpeciesCarica papaya (Papaya)
E.C. Number (IntEnz) 3.4.22.2
CSA Homologues of 9papThere are 198 Homologs
CSA Entries With UniProtID P00784
CSA Entries With EC Number 3.4.22.2
PDBe Entry 9pap
PDBSum Entry 9pap
MACiE Entry M0174

Literature Report

Introduction The thiol protease family is a large, well-studied group with a well-known "catalytic triad" motif.
Mechansim In the case of the peptidases, the reaction is a hydrolysis of a peptide, ester, thio-ester or thiono-ester bond, via a covalent intermediate, resulting from nucleophilic attack of the active-site thiol group on the carbonyl carbon of the amide or ester scissile bond.
The factor XIII EC 2.3.2.13 forms an amide link between lysine and glutamine residues on the two substrates. This is essentially the peptidase activity in reverse.

Catalytic Sites for 9pap

Annotated By Reference To The Literature - Site 3 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AsnA175308macie:sideChain
GlnA19152macie:sideChain
OcsA25158macie:ptm
HisA159292macie:sideChain

Annotated By Reference To The Literature - Site 4 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AsnA175308macie:sideChain
GlnA19152macie:sideChain
OcsA25158macie:ptm
HisA159292macie:sideChain

Literature References

Notes:
Pedersen LC
Transglutaminase factor XIII uses proteinase-like catalytic triad to crosslink macromolecules.
Protein Sci 1994 3 1131-1135
PubMed: 7920263
Storer AC
Catalytic mechanism in papain family of cysteine peptidases.
Methods Enzymol 1994 244 486-500
PubMed: 7845227
Johnston SC
Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 A resolution.
EMBO J 1997 16 3787-3796
PubMed: 9233788
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