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Catalytic Site Atlas

CSA LITERATURE entry for 1k30

E.C. nameglycerol-3-phosphate O-acyltransferase
SpeciesCucurbita moschata ()
E.C. Number (IntEnz) 2.3.1.15
CSA Homologues of 1k301iuq,
CSA Entries With UniProtID P10349
CSA Entries With EC Number 2.3.1.15
PDBe Entry 1k30
PDBSum Entry 1k30
MACiE Entry 1k30

Literature Report

IntroductionGlycerol-3-phosphate (1)-acyltransferase (G3PAT) catalyses the attachment of an acyl group from either acyl-carrier proteins (acyl-ACPs) or acyl-CoAs onto the C1 hydroxyl group of glycerol-3-phosphate to give 1-acylglycerol-3-phosphate. Different G3PAT enzymes have different substrate specificities, with some preferring to add the unsaturated fatty acid oleate and others using both oleate and the saturated fatty acid palmitate. The different substrate specificities within this family has been implicated in the sensitivity of plants to chilling temperatures.
MechansimGlycerol-3-phosphate (1)-acyltransferase is thought to employ a His-Asp dyad resembling that of serine proteases. His 139 acts to deprotonate the C1 hydroxyl group of glycerol-3-phosphate, allowing nucleophilic attack by this group on the carbonyl of acyl-ACP or acyl-CoA. Asp 144 serves to modify the pKa of His 139, allowing it to act as a catalytic base.
Reaction

Catalytic Sites for 1k30

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
HisA139167macie:sideChainProposed to deprotonate the C1 hydroxyl group of glycerol 3-phosphate, allowing this group to attack the fatty acyl substrate.
AspA144172macie:sideChainProposed to modify the pKa of His 139, allowing it to act as a catalytic base.

Literature References

Notes:
Turnbull AP
Analysis of the structure, substrate specificity, and mechanism of squash glycerol-3-phosphate (1)-acyltransferase.
Structure 2001 9 347-353
PubMed: 11377195
Heath RJ
A conserved histidine is essential for glycerolipid acyltransferase catalysis.
J Bacteriol 1998 180 1425-1430
PubMed: 9515909
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