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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1hv9

E.C. nameglucosamine-1-phosphate N-acetyltransferase
SpeciesEscherichia coli (Bacteria)
E.C. Number (IntEnz) 2.3.1.157
CSA Homologues of 1hv9There are 83 Homologs
CSA Entries With UniProtID P0ACC7
CSA Entries With EC Number 2.3.1.157
PDBe Entry 1hv9
PDBSum Entry 1hv9
MACiE Entry 1hv9

Literature Report

IntroductionThe bifunctional enzyme N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE is able to catalyse two steps in the pathway of bacterial cell wall synthesis. In the first step carried out by the enzyme glucosamine-1-phosphate is converted to N acetyl glucosamine-1-phosphate using Acetyl coA as the donor. In the second step UTP is used to activate the n acetyl glucosamine-1-phosphate forming UDP acetyl glucosamine and Pyrophosphate. Interest in the processes catalysed by this enzyme stems from its potential as an antibiotic target. The first step is carried out by the C terminal domain, whilst the second step, described here, is carried out by an active site in the N terminal domain.
MechansimThe mechanism of the transfer of UDP to N acetylglucosamine-1-phosphate proceeds via nucleophilic attack from the phosphate oxygen of the phosphate moiety on the alpha phosphate producing a pentavalent phosphate transition state. This is stabilised by Mg2+ at the active site and Arg 18, and collapses to release the beta and gamma phosphates as pyrophosphate.
Reaction

Catalytic Sites for 1hv9

Annotated By Reference To The Literature - Site 3 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ArgA1818macie:sideChainStabilises the transition state by forming electrostatic contacts to the alpha phosphate of UTP.

Annotated By Reference To The Literature - Site 4 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ArgB1818macie:sideChainStabilises the transition state by forming electrostatic contacts to the alpha phosphate of UTP.

Literature References

Notes:
Brown K
Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily.
EMBO J 1999 18 4096-4107
PubMed: 10428949
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