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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1ast

E.C. nameastacin
SpeciesAstacus fluviatilis (Astacus astacus)
E.C. Number (IntEnz) 3.4.24.21
CSA Homologues of 1astThere are 11 Homologs
CSA Entries With UniProtID P07584
CSA Entries With EC Number 3.4.24.21
PDBe Entry 1ast
PDBSum Entry 1ast
MACiE Entry 1ast

Literature Report

IntroductionAstacin, a digestive zinc-endopeptidase from the crayfish Astacus astacus, is the prototype for the 'astacin family', which includes mammalian metallo-endopeptidases and developmentally regulated proteins of human, fruitfly, frog and sea urchin, and also for the 'metzincin superfamily'.
MechansimA zinc-activated water molecule is deprotonated by glutamate, and then carries out a nucleophilic attack on the substrate. A tyrosine residue stabilises the transition state.
Reaction

Catalytic Sites for 1ast

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluA93142macie:sideChainDeprotonates the catalytic water molecule, protonates the amide leaving group.
TyrA149198macie:sideChainStabilises the transition state.

Literature References

Notes:
Guevara T
Proenzyme structure and activation of astacin metallopeptidase.
J Biol Chem 2010 285 13958-13965
PubMed: 20202938
Yiallouros I
The roles of Glu93 and Tyr149 in astacin-like zinc peptidases.
FEBS Lett 2000 484 224-228
PubMed: 11078883
Rawlings ND
Evolutionary families of metallopeptidases.
Methods Enzymol 1995 248 183-228
PubMed: 7674922
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