Crystal Structures of Two Bacterial 3-Hydroxy-3-methylglutaryl-CoA Lyases Suggest a Common Catalytic Mechanism among a Family of TIM Barrel Metalloenzymes Cleaving Carbon-Carbon Bonds-Reference-Cited by-同舟云学术

Crystal Structures of Two Bacterial 3-Hydroxy-3-methylglutaryl-CoA Lyases Suggest a Common Catalytic Mechanism among a Family of TIM Barrel Metalloenzymes Cleaving Carbon-Carbon Bonds

Published:2006-03 Issue:11 Volume:281 Page:7533-7545
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Forouhar Farhad,Hussain Munif,Farid Ramy,Benach Jordi,Abashidze Mariam,Edstrom William C.,Vorobiev Sergey M.,Xiao Rong,Acton Thomas B.,Fu Zhuji,Kim Jung-Ja P.,Miziorko Henry M.,Montelione Gaetano T.,Hunt John F.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference47 articles.

1. Biochemical and molecular analyses in three patients with 3-hydroxy-3-methylglutaric aciduria

2. Molecular basis of 3-hydroxy-3-methylglutaric aciduria

3. 3-hydroxy-3-methylglutaryl-coenzyme A lyase deficiency: review of 18 reported patients

4. Molecular prenatal diagnosis of 3-hydroxy−3-methylglutaryl coa lyase deficiency

5. The E37X is a common HMGCL mutation in Portuguese patients with 3-hydroxy-3-methylglutaric CoA lyase deficiency

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