The structural basis for the UDP-sugar selectivity of human UDP-glycosyltransferase 2B7 (UGT2B7): A combined computational and experimental approach

Pramod C. Nair; Nuy Chau; Ross A. McKinnon; John O. Miners

The structural basis for the UDP-sugar selectivity of human UDP-glycosyltransferase 2B7 (UGT2B7): A combined computational and experimental approach

Pramod C. Nair, Nuy Chau, Ross A. McKinnon, John O. Miners

College of Medicine and Public Health

Research output: Contribution to conference › Abstract › peer-review

Abstract

Introduction. Enzymes of the human uridine diphosphate (UDP)-glycosyltransferase (UGT) superfamily catalyse the covalent addition of the sugar moiety from a UDP-sugar cofactor to relatively low molecular weight lipophilic substrates. UGT2B7 can utilise both UDP-glucuronic acid (UDP-GlcUA) and UDP-glucose (UDP-Glc) as cofactors. However, glucuronidation is the preferred metabolic pathway. Currently, it is unclear which residues in the UGT2B7 cofactor binding domain are responsible for the preferential binding of UDP-GlcUA.

Original language	English
Number of pages	1
Publication status	Published - 2020

Keywords

uridine diphosphate
glycosyltransferase
UDP-sugar
Enzymes
glucuronidation

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title = "The structural basis for the UDP-sugar selectivity of human UDP-glycosyltransferase 2B7 (UGT2B7): A combined computational and experimental approach",

abstract = "Introduction. Enzymes of the human uridine diphosphate (UDP)-glycosyltransferase (UGT) superfamily catalyse the covalent addition of the sugar moiety from a UDP-sugar cofactor to relatively low molecular weight lipophilic substrates. UGT2B7 can utilise both UDP-glucuronic acid (UDP-GlcUA) and UDP-glucose (UDP-Glc) as cofactors. However, glucuronidation is the preferred metabolic pathway. Currently, it is unclear which residues in the UGT2B7 cofactor binding domain are responsible for the preferential binding of UDP-GlcUA.",

keywords = "uridine diphosphate, glycosyltransferase, UDP-sugar, Enzymes, glucuronidation",

author = "Nair, {Pramod C.} and Nuy Chau and McKinnon, {Ross A.} and Miners, {John O.}",

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TY - CONF

T1 - The structural basis for the UDP-sugar selectivity of human UDP-glycosyltransferase 2B7 (UGT2B7)

T2 - A combined computational and experimental approach

AU - Nair, Pramod C.

AU - Chau, Nuy

AU - McKinnon, Ross A.

AU - Miners, John O.

PY - 2020

Y1 - 2020

N2 - Introduction. Enzymes of the human uridine diphosphate (UDP)-glycosyltransferase (UGT) superfamily catalyse the covalent addition of the sugar moiety from a UDP-sugar cofactor to relatively low molecular weight lipophilic substrates. UGT2B7 can utilise both UDP-glucuronic acid (UDP-GlcUA) and UDP-glucose (UDP-Glc) as cofactors. However, glucuronidation is the preferred metabolic pathway. Currently, it is unclear which residues in the UGT2B7 cofactor binding domain are responsible for the preferential binding of UDP-GlcUA.

AB - Introduction. Enzymes of the human uridine diphosphate (UDP)-glycosyltransferase (UGT) superfamily catalyse the covalent addition of the sugar moiety from a UDP-sugar cofactor to relatively low molecular weight lipophilic substrates. UGT2B7 can utilise both UDP-glucuronic acid (UDP-GlcUA) and UDP-glucose (UDP-Glc) as cofactors. However, glucuronidation is the preferred metabolic pathway. Currently, it is unclear which residues in the UGT2B7 cofactor binding domain are responsible for the preferential binding of UDP-GlcUA.

KW - uridine diphosphate

KW - glycosyltransferase

KW - UDP-sugar

KW - Enzymes

KW - glucuronidation

UR - https://www.asceptasm.com/2020-annual-scientific-meeting/program-workshops/

M3 - Abstract

ER -

The structural basis for the UDP-sugar selectivity of human UDP-glycosyltransferase 2B7 (UGT2B7): A combined computational and experimental approach

Abstract

Keywords

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