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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1hr7

E.C. namemitochondrial processing peptidase
SpeciesSaccharomyces cerevisiae (Baker's yeast)
E.C. Number (IntEnz) 3.4.24.64
CSA Homologues of 1hr7There are 60 Homologs
CSA Entries With UniProtID P11914
CSA Entries With EC Number 3.4.24.64
PDBe Entry 1hr7
PDBSum Entry 1hr7
MACiE Entry 1hr7

Literature Report

IntroductionMitochondrial processing peptidase is a metalloendopeptidase which cleaves the N-terminal signal sequence of nuclear encoded proteins directed to the mitochondrion from the cytoplasm.
MechansimThe mechanism of mitochondrial processing peptidase occurs in a thermolysin-like general-base-type mechanism. The zinc ion co-ordinates water which is displaced in substrate coordination towards Glu beta-73 which acts via general base catalysis to activate the water oxygen for nucleophilic attack on the carbonyl carbon of the scissile bond. The zinc ion also has a role in activating the water molecule by coordinating the oxygen. The pentacoordinate intermediate is formed and the proton accepted by Glu beta-73 in activating water is then transferred to the leaving nitrogen to facilitate collapse of the intermediate. A second proton transfer then occurs to shuttle a proton from the hydrated peptide to the leaving nitrogen.
Reaction

Catalytic Sites for 1hr7

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GlnB7373macie:sideChainActs as a general acid/base catalyst in activating water for nucleophilic attack and collapse of intermediates through proton transfer to facilitate loss of the leaving group.

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GlnD7373macie:sideChainActs as a general acid/base catalyst in activating water for nucleophilic attack and collapse of intermediates through proton transfer to facilitate loss of the leaving group.

Annotated By Reference To The Literature - Site 3 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GlnF7373macie:sideChainActs as a general acid/base catalyst in activating water for nucleophilic attack and collapse of intermediates through proton transfer to facilitate loss of the leaving group.

Annotated By Reference To The Literature - Site 4 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GlnH7373macie:sideChainActs as a general acid/base catalyst in activating water for nucleophilic attack and collapse of intermediates through proton transfer to facilitate loss of the leaving group.

Annotated By Reference To The Literature - Site 5 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AspA6565macie:sideChainActs as a general acid/base catalyst in activating water for nucleophilic attack and collapse of intermediates through proton transfer to facilitate loss of the leaving group.

Annotated By Reference To The Literature - Site 6 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AspC6565macie:sideChainActs as a general acid/base catalyst in activating water for nucleophilic attack and collapse of intermediates through proton transfer to facilitate loss of the leaving group.

Annotated By Reference To The Literature - Site 7 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AspE6565macie:sideChainActs as a general acid/base catalyst in activating water for nucleophilic attack and collapse of intermediates through proton transfer to facilitate loss of the leaving group.

Annotated By Reference To The Literature - Site 8 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AspG6565macie:sideChainActs as a general acid/base catalyst in activating water for nucleophilic attack and collapse of intermediates through proton transfer to facilitate loss of the leaving group.

Literature References

Notes:
Taylor AB
Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences.
Structure 2001 9 615-625
PubMed: 11470436
Makarova KS
Thermolysin and mitochondrial processing peptidase: how far structure-functional convergence goes.
Protein Sci 1999 8 2537-2540
PubMed: 10595562
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