Crystal Structure-Based Analysis of Human Glucuronyltransferase 1

Lars C. Pedersen, Thomas A. Darden, Yoshimitsu Kakuta, Masahiko Negishi

Research output: Contribution to journalReview article

Abstract

Glucuronyltransferase I (GlcAT-I) is a key enzyme in heparan/chondroitin biosynthesis (1). The X-ray crystal structure of human GlcAT-1 has been solved in the presence of both UDP and substrate analog. The structure reveals a two sub-domain structure known as the SGC domain. Donor substrate-binding site resides in the N-terminal sub-domain, while acceptor substrate-binding site is located in the C-terminal sub-domain. In addition to conserved residues responsible for the donor binding, various residues that interact with the acceptor molecule have now been identified. The GlcAT-1 provides the structural basis for understanding the structure and function of glycosyltransferases.

Original languageEnglish
Pages (from-to)121-129
Number of pages9
JournalTrends in Glycoscience and Glycotechnology
Volume13
Issue number70
DOIs
Publication statusPublished - Jan 1 2001
Externally publishedYes

Fingerprint

Glucuronosyltransferase
Crystal structure
Binding Sites
Chondroitin
Glycosyltransferases
Uridine Diphosphate
Substrates
Biosynthesis
X-Rays
Enzymes
X rays
Molecules
galactosylgalactoylxylosylprotein 3-beta-glucuronosyltransferase

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Organic Chemistry

Cite this

Crystal Structure-Based Analysis of Human Glucuronyltransferase 1. / Pedersen, Lars C.; Darden, Thomas A.; Kakuta, Yoshimitsu; Negishi, Masahiko.

In: Trends in Glycoscience and Glycotechnology, Vol. 13, No. 70, 01.01.2001, p. 121-129.

Research output: Contribution to journalReview article

Pedersen, Lars C. ; Darden, Thomas A. ; Kakuta, Yoshimitsu ; Negishi, Masahiko. / Crystal Structure-Based Analysis of Human Glucuronyltransferase 1. In: Trends in Glycoscience and Glycotechnology. 2001 ; Vol. 13, No. 70. pp. 121-129.
@article{d2a83f28b7864c679b16f3daeb35773f,
title = "Crystal Structure-Based Analysis of Human Glucuronyltransferase 1",
abstract = "Glucuronyltransferase I (GlcAT-I) is a key enzyme in heparan/chondroitin biosynthesis (1). The X-ray crystal structure of human GlcAT-1 has been solved in the presence of both UDP and substrate analog. The structure reveals a two sub-domain structure known as the SGC domain. Donor substrate-binding site resides in the N-terminal sub-domain, while acceptor substrate-binding site is located in the C-terminal sub-domain. In addition to conserved residues responsible for the donor binding, various residues that interact with the acceptor molecule have now been identified. The GlcAT-1 provides the structural basis for understanding the structure and function of glycosyltransferases.",
author = "Pedersen, {Lars C.} and Darden, {Thomas A.} and Yoshimitsu Kakuta and Masahiko Negishi",
year = "2001",
month = "1",
day = "1",
doi = "10.4052/tigg.13.121",
language = "English",
volume = "13",
pages = "121--129",
journal = "Trends in Glycoscience and Glycotechnology",
issn = "0915-7352",
publisher = "Gakushin Publishing Company",
number = "70",

}

TY - JOUR

T1 - Crystal Structure-Based Analysis of Human Glucuronyltransferase 1

AU - Pedersen, Lars C.

AU - Darden, Thomas A.

AU - Kakuta, Yoshimitsu

AU - Negishi, Masahiko

PY - 2001/1/1

Y1 - 2001/1/1

N2 - Glucuronyltransferase I (GlcAT-I) is a key enzyme in heparan/chondroitin biosynthesis (1). The X-ray crystal structure of human GlcAT-1 has been solved in the presence of both UDP and substrate analog. The structure reveals a two sub-domain structure known as the SGC domain. Donor substrate-binding site resides in the N-terminal sub-domain, while acceptor substrate-binding site is located in the C-terminal sub-domain. In addition to conserved residues responsible for the donor binding, various residues that interact with the acceptor molecule have now been identified. The GlcAT-1 provides the structural basis for understanding the structure and function of glycosyltransferases.

AB - Glucuronyltransferase I (GlcAT-I) is a key enzyme in heparan/chondroitin biosynthesis (1). The X-ray crystal structure of human GlcAT-1 has been solved in the presence of both UDP and substrate analog. The structure reveals a two sub-domain structure known as the SGC domain. Donor substrate-binding site resides in the N-terminal sub-domain, while acceptor substrate-binding site is located in the C-terminal sub-domain. In addition to conserved residues responsible for the donor binding, various residues that interact with the acceptor molecule have now been identified. The GlcAT-1 provides the structural basis for understanding the structure and function of glycosyltransferases.

UR - http://www.scopus.com/inward/record.url?scp=0345861046&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0345861046&partnerID=8YFLogxK

U2 - 10.4052/tigg.13.121

DO - 10.4052/tigg.13.121

M3 - Review article

VL - 13

SP - 121

EP - 129

JO - Trends in Glycoscience and Glycotechnology

JF - Trends in Glycoscience and Glycotechnology

SN - 0915-7352

IS - 70

ER -