i.e. 3',7'-dihydroxy-5'-cholanoic acid. The enzyme uses ursodeoxycholic acid and UDP N-acetylglucosamine in preference to other primary and secondary bile acids, and other UDP sugars such as UDP glucose, UDP glucuronic acid, UDP galactose, and UDP xylose
multispecies sequence analysis reveals that only primates possess UGT3A sequences containing residue Asn391, suggesting that other mammals may not have the capacity to N-acetylglucosaminidate small molecules. In support of this hypothesis, Asn391-containing UGT3A forms from two non-human primates are found to use UDP-GlcNAc, whereas UGT3A isoforms from non-primates can could not use this sugar donor
multispecies sequence analysis reveals that only primates possess UGT3A sequences containing residue Asn391, suggesting that other mammals may not have the capacity to N-acetylglucosaminidate small molecules. In support of this hypothesis, Asn391-containing UGT3A forms from two non-human primates are found to use UDP-GlcNAc, whereas UGT3A isoforms from non-primates can could not use this sugar donor
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of homology models docked with UDP-sugar donors indicates that residue N391 in UGT3A1 is able to accommodate the N-acetyl group on C2 of UDP-GlcNAc so that the anomeric carbon atom C1 is optimally situated for catalysis involving residue His35. Replacement of Asn with Phe at position 391 disrupts this catalytically productive orientation of UDP-GlcNAc but allows a more optimal alignment of UDP-Glc for sugar donation
residue N391 is necessary for utilization of UDP-GlcNAc as substrate. Mutation N391F in UGT3A1 enhances its ability to utilize UDP-Glc and completely inhibits its ability to use UDP-GlcNAc. An analysis of homology models docked with UDP-sugar donors indicates that N391 in UGT3A1 is able to accommodate the N-acetyl group on C2 of UDP-GlcNAc so that the anomeric carbon atom C1 is optimally situated for catalysis involving residue His35. Replacement of Asn with Phe at position 391 disrupts this catalytically productive orientation of UDP-GlcNAc but allows a more optimal alignment of UDP-Glc for sugar donation
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2.4.1.B7 ursodeoxycholate N-acetylglucosaminyltransferase
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