(Q46935096)

English

Identification of aspartic acid and histidine residues mediating the reaction mechanism and the substrate specificity of the human UDP-glucuronosyltransferases 1A.

scientific article published on 23 October 2007

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scholarly article

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Europe PubMed Central

PubMed publication ID

26 December 2017

http://europepmc.org/abstract/MED/17956868

Identification of aspartic acid and histidine residues mediating the reaction mechanism and the substrate specificity of the human UDP-glucuronosyltransferases 1A. (English)

1 reference

Europe PubMed Central

PubMed publication ID

26 December 2017

http://europepmc.org/abstract/MED/17956868

Jacques Magdalou

6

object named as

Jacques Magdalou

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Europe PubMed Central

PubMed publication ID

26 December 2017

http://europepmc.org/abstract/MED/17956868

author name string

Dong Li

1

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Europe PubMed Central

PubMed publication ID

26 December 2017

http://europepmc.org/abstract/MED/17956868

Sylvie Fournel-Gigleux

2

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Europe PubMed Central

PubMed publication ID

26 December 2017

http://europepmc.org/abstract/MED/17956868

Lydia Barré

3

1 reference

Europe PubMed Central

PubMed publication ID

26 December 2017

http://europepmc.org/abstract/MED/17956868

Guillermo Mulliert

4

1 reference

Europe PubMed Central

PubMed publication ID

26 December 2017

http://europepmc.org/abstract/MED/17956868

Patrick Netter

5

1 reference

Europe PubMed Central

PubMed publication ID

26 December 2017

http://europepmc.org/abstract/MED/17956868

Mohamed Ouzzine

7

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26 December 2017

http://europepmc.org/abstract/MED/17956868

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publication date

23 October 2007

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Europe PubMed Central

PubMed publication ID

26 December 2017

http://europepmc.org/abstract/MED/17956868

Journal of Biological Chemistry

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PubMed publication ID

26 December 2017

http://europepmc.org/abstract/MED/17956868

282

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PubMed publication ID

26 December 2017

http://europepmc.org/abstract/MED/17956868

50

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PubMed publication ID

26 December 2017

http://europepmc.org/abstract/MED/17956868

36514-36524

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Europe PubMed Central

PubMed publication ID

26 December 2017

http://europepmc.org/abstract/MED/17956868

A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities

1 reference

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1 reference

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UDP-glucuronosyltransferases and clinical drug-drug interactions

1 reference

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21 January 2018

Structural and functional studies of UDP-glucuronosyltransferases

1 reference

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UDP-glucuronosyltransferases: a family of detoxifying enzymes

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Crystal structure of the cofactor-binding domain of the human phase II drug-metabolism enzyme UDP-glucuronosyltransferase 2B7

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Crystal structures of the T4 phage beta-glucosyltransferase and the D100A mutant in complex with UDP-glucose: glucose binding and identification of the catalytic base for a direct displacement mechanism

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Chemical modification of human UDP-glucuronosyltransferase UGT1*6 by diethyl pyrocarbonate: possible involvement of a histidine residue in the catalytic process.

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21 January 2018

The chemical modification of human liver UDP-glucuronosyltransferase UGT1*6 reveals the involvement of a carboxyl group in catalysis

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21 January 2018

E. Coli MurG: a paradigm for a superfamily of glycosyltransferases

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Structure of the UDP-glucosyltransferase GtfB that modifies the heptapeptide aglycone in the biosynthesis of vancomycin group antibiotics

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21 January 2018

The UDP glycosyltransferase gene superfamily: recommended nomenclature update based on evolutionary divergence

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21 January 2018

A critical amino acid residue, asp446, in UDP-glucuronosyltransferase.

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21 January 2018

Expression and functional domains of rabbit liver UDP-glucuronosyltransferase 2B16 and 2B13.

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21 January 2018

Substrate positioning by His92 is important in catalysis by purple acid phosphatase

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21 January 2018

Discovery of a substrate selectivity switch in tyrosine ammonia-lyase, a member of the aromatic amino acid lyase family

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21 January 2018

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

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Identifiers

10.1074/JBC.M703107200

1 reference

Europe PubMed Central

PubMed publication ID

26 December 2017

http://europepmc.org/abstract/MED/17956868

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

26 December 2017

http://europepmc.org/abstract/MED/17956868

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