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Catalytic Site Atlas

CSA LITERATURE entry for 1ge7

E.C. namepeptidyl-Lys metalloendopeptidase
SpeciesGrifola frondosa (Maitake)
E.C. Number (IntEnz) 3.4.24.20
CSA Homologues of 1ge71eb6,1g12,1ge5,1ge6,
CSA Entries With UniProtID P81054
CSA Entries With EC Number 3.4.24.20
PDBe Entry 1ge7
PDBSum Entry 1ge7
MACiE Entry 1ge7

Literature Report

IntroductionMetalloendopeptidases such as the zinc endopeptidases often have the potential for tissue destruction or pathogenic bacterial infections and so are targets for drug design.
MechansimThe zinc peptidase catalyses hydrolysis of proteins. Glu 118 and Zn together act to activate a water molecule so that it can act as a nucleophile to attack the peptide substrate. This forms a tetrahedral intermediate, stabilised by "proton donation" by Tyr 133, which then collapses to release the products.
Reaction

Catalytic Sites for 1ge7

Annotated By Reference To The Literature - Site 3 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluA118299macie:sideChainActs as a general acid/base catalyst to activate the water for nucleophilic attack and facilitate collapse of the tetrahedral intermediate by proton donation.
TyrA133314macie:sideChainStabilises the tetrahedral intermediate.

Annotated By Reference To The Literature - Site 4 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluB118299macie:sideChainActs as a general acid/base catalyst to activate the water for nucleophilic attack and facilitate collapse of the tetrahedral intermediate by proton donation.
TyrB133314macie:sideChainStabilises the tetrahedral intermediate.

Literature References

Notes:
Hori T
Structure of a new 'aspzincin' metalloendopeptidase from Grifola frondosa: implications for the catalytic mechanism and substrate specificity based on several different crystal forms.
Acta Crystallogr D Biol Crystallogr 2001 57 361-368
PubMed: 11223512
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