Structural, functional, and mutagenesis studies of UDP-glycosyltransferases

Vatsala Malik; Gary Black

doi:10.1016/B978-0-12-398312-1.00004-4

Structural, functional, and mutagenesis studies of UDP-glycosyltransferases

Vatsala Malik, Gary Black

Research output: Contribution to journal › Article › peer-review

19 Citations (Scopus)

Abstract

The biosynthesis of the complex carbohydrates that govern many cellular functions requires the action of a diverse range of selective glycosyltransferases (GTs). Uridine diphosphate sugar-utilizing GTs (UGTs) account for the majority of characterized GTs. GTs have been classified into families (currently 92) based on amino-acid sequence similarity. However, as amino-acid sequence similarity cannot reliable predict catalytic mechanism, GTs have also been grouped into four clans based on catalytic mechanism and structural fold. GTs catalyze glycosidic bond formation with two possible stereochemical outcomes: inversion or retention of anomeric configuration. All UGTs also belong to one of two distinct structural folds, GT-A and GT-B. UGTs have conserved residues that are associated with nucleotide diphosphate sugar recognition and acceptor recognition. UGT diversification has been performed using in vitro DNA recombination, domain swapping, and random mutagenesis.

Original language	English
Pages (from-to)	87-115
Journal	Advances in Protein Chemistry and Structural Biology
Volume	87
DOIs	https://doi.org/10.1016/B978-0-12-398312-1.00004-4
Publication status	Published - 2012

Keywords

catalytic mechanism
structural fold
anomeric configuration

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10.1016/B978-0-12-398312-1.00004-4

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abstract = "The biosynthesis of the complex carbohydrates that govern many cellular functions requires the action of a diverse range of selective glycosyltransferases (GTs). Uridine diphosphate sugar-utilizing GTs (UGTs) account for the majority of characterized GTs. GTs have been classified into families (currently 92) based on amino-acid sequence similarity. However, as amino-acid sequence similarity cannot reliable predict catalytic mechanism, GTs have also been grouped into four clans based on catalytic mechanism and structural fold. GTs catalyze glycosidic bond formation with two possible stereochemical outcomes: inversion or retention of anomeric configuration. All UGTs also belong to one of two distinct structural folds, GT-A and GT-B. UGTs have conserved residues that are associated with nucleotide diphosphate sugar recognition and acceptor recognition. UGT diversification has been performed using in vitro DNA recombination, domain swapping, and random mutagenesis.",

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T1 - Structural, functional, and mutagenesis studies of UDP-glycosyltransferases

AU - Malik, Vatsala

AU - Black, Gary

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AB - The biosynthesis of the complex carbohydrates that govern many cellular functions requires the action of a diverse range of selective glycosyltransferases (GTs). Uridine diphosphate sugar-utilizing GTs (UGTs) account for the majority of characterized GTs. GTs have been classified into families (currently 92) based on amino-acid sequence similarity. However, as amino-acid sequence similarity cannot reliable predict catalytic mechanism, GTs have also been grouped into four clans based on catalytic mechanism and structural fold. GTs catalyze glycosidic bond formation with two possible stereochemical outcomes: inversion or retention of anomeric configuration. All UGTs also belong to one of two distinct structural folds, GT-A and GT-B. UGTs have conserved residues that are associated with nucleotide diphosphate sugar recognition and acceptor recognition. UGT diversification has been performed using in vitro DNA recombination, domain swapping, and random mutagenesis.

KW - catalytic mechanism

KW - structural fold

KW - anomeric configuration

U2 - 10.1016/B978-0-12-398312-1.00004-4

DO - 10.1016/B978-0-12-398312-1.00004-4

M3 - Article

SN - 1876-1623

VL - 87

SP - 87

EP - 115

JO - Advances in Protein Chemistry and Structural Biology

JF - Advances in Protein Chemistry and Structural Biology

ER -

Structural, functional, and mutagenesis studies of UDP-glycosyltransferases

Abstract

Keywords

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