Literature summary for 2.4.1.B7 extracted from

Meech, R.; Rogers, A.; Zhuang, L.; Lewis, B.C.; Miners, J.O.; Mackenzie, P.I.
Identification of residues that confer sugar selectivity to UDP-glycosyltransferase 3A (UGT3A) enzymes (2012), J. Biol. Chem., 287, 24122-24130.

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Homo sapiens

Crystallization (Comment)

Organism

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

Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
N391F	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	Homo sapiens

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
0.00175	-	UDP-D-glucose	wild-type, pH 7.5, 37°C	Homo sapiens
0.015	-	UDP-D-glucose	mutant N391F, pH 7.5, 37°C	Homo sapiens
0.065	-	UDP-N-acetyl-D-glucosamine	wild-type, pH 7.5, 37°C	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-
Pan troglodytes	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
UDP-D-glucose + ursodeoxycholate	-	Homo sapiens	UDP + 7beta-D-glucosyl-ursodeoxycholate	-	?
UDP-N-acetyl-D-glucosamine + ursodeoxycholate	-	Homo sapiens	UDP + 7beta-(N-acetyl-D-glucosaminyl)-ursodeoxycholate	-	?
UDP-N-acetyl-D-glucosamine + ursodeoxycholate	-	Pan troglodytes	UDP + 7beta-(N-acetyl-D-glucosaminyl)-ursodeoxycholate	-	?

Synonyms

Synonyms	Comment	Organism
UGT3A1	-	Homo sapiens
UGT3A1	-	Pan troglodytes

General Information

General Information	Comment	Organism
physiological function	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	Homo sapiens
physiological function	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	Pan troglodytes