Glyoxylate carboligase lacks the canonical active site glutamate of thiamine-dependent enzymes-Reference-Cited by-同舟云学术

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Glyoxylate carboligase lacks the canonical active site glutamate of thiamine-dependent enzymes

Published:2008-01-06 Issue:2 Volume:4 Page:113-118
ISSN:1552-4450
Container-title:Nature Chemical Biology
language:en
Short-container-title:Nat Chem Biol

Author:

Kaplun Alexander,Binshtein Elad,Vyazmensky Maria,Steinmetz Andrea,Barak Ze'ev,Chipman David M,Tittmann Kai,Shaanan Boaz

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Molecular Biology

Link

http://www.nature.com/articles/nchembio.62.pdf

Reference44 articles.

1. Muller, Y.A. et al. A thiamin diphosphate binding fold revealed by comparison of the crystal structures of transketolase, pyruvate oxidase and pyruvate decarboxylase. Structure 1, 95–103 (1993).

2. Kern, D. et al. How thiamine diphosphate is activated in enzymes. Science 275, 67–70 (1997).

3. Breslow, R. On the mechanism of thiamine action: IV. Evidence from studies on model systems. J. Am. Chem. Soc. 80, 3719–3726 (1958).

4. Schellenberger, A. Structure and mechanism of action of the active center of yeast pyruvate decarboxylase. Angew. Chem. Int. Ed. Engl. 6, 1024–1035 (1967).

5. Wille, G. et al. The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography. Nat. Chem. Biol. 2, 324–328 (2006).

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