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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1chm

E.C. namecreatinase
SpeciesPseudomonas putida (Bacteria)
E.C. Number (IntEnz) 3.5.3.3
CSA Homologues of 1chm1kp0,1qxw,1qxy,
CSA Entries With UniProtID P38488
CSA Entries With EC Number 3.5.3.3
PDBe Entry 1chm
PDBSum Entry 1chm
MACiE Entry M0096

Literature Report

IntroductionCreatinase catalyses the hydrolysis of creatine to sarcosine and urea. This is a key step in the metabolic breakdown of creatinine by micro-organisms. Creatinase is also found in higher animals but its metabolic role is as yet not known.
MechansimHistidine 232 abstracts a proton from an active site water molecule to create a hydroxide nucleophile. Glutamate 262 and 358 are negatively charged and break the resonance of the guanidinium group, this allows the hydroxide to attack at C1. Histidine 232 now donates its proton to N3 which leads to the C1-N3 bond breaking. Histidine 232 again abstracts a proton, this time from the hydroxide attached to C1, leaving the reaction products urea and sarcosine.
Reaction

Catalytic Sites for 1chm

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
HisA232232macie:sideChainThe residue acts as a general base to the hydrolytic water molecule, a general acid to the intermediate, and then as a base once more in a heterolytic bimolecular elimination reaction, leading to the products.
GluA262262macie:sideChainThe residue's charged side chain breaks the resonance of the creatine gaunidinium group, allowing the hydroxyl to act as a nucleophile at the partial carbocation.
GluA358358macie:sideChainThe residue's charged side chain breaks the resonance of the creatine gaunidinium group, allowing the hydroxyl to act as a nucleophile at the partial carbocation.

Literature References

Notes:
Coll M
Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal structures.
J Mol Biol 1990 214 597-610
PubMed: 1696320
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