The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families-Reference-Cited by-同舟云学术

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The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families

Published:1996-01 Issue:1 Volume:3 Page:74-86
ISSN:1072-8368
Container-title:Nature Structural Biology
language:
Short-container-title:Nat Struct Mol Biol

Author:

Tesmer John J.G.,Klem Thomas J.,Deras Michael L.,Davisson V. Jo,Smith Janet L.

Publisher

Springer Science and Business Media LLC

Subject

Genetics,Biochemistry,Structural Biology

Reference68 articles.

1. Three-dimensional structure of the tryptophan synthase alpha 2 beta 2 multienzyme complex from Salmonella typhimurium.

2. Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains.

3. A Separate Antibiotic-binding Site in Xanthosine-5'-phosphate Aminase: Inhibitor- and Substrate-binding Studies*

4. Positional isotope exchange and kinetic experiments with Escherichia coli guanosine 5'-monophosphate synthetase

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