Glyoxylate Carboligase: A Unique Thiamin Diphosphate-Dependent Enzyme That Can Cycle between the 4′-Aminopyrimidinium and 1′,4′-Iminopyrimidine Tautomeric Forms in the Absence of the Conserved Glutamate-Reference-Cited by-同舟云学术

Glyoxylate Carboligase: A Unique Thiamin Diphosphate-Dependent Enzyme That Can Cycle between the 4′-Aminopyrimidinium and 1′,4′-Iminopyrimidine Tautomeric Forms in the Absence of the Conserved Glutamate

Published:2012-09-25 Issue:40 Volume:51 Page:7940-7952
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Nemeria Natalia¹,Binshtein Elad²,Patel Hetalben¹,Balakrishnan Anand¹,Vered Ilan²,Shaanan Boaz²,Barak Ze’ev²,Chipman David²,Jordan Frank¹

Affiliation:

1. Department of Chemistry, Rutgers University, 73 Warren Street, Newark, New Jersey 07102, United States

2. Department of Life Sciences, Ben-Gurion University, P.O. Box 653, Beer-Sheva 84105, Israel

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi300893v

Reference36 articles.

1. Molecular cloning, DNA sequencing, and biochemical analyses of Escherichia coli glyoxylate carboligase. An enzyme of the acetohydroxy acid synthase-pyruvate oxidase family.

2. Glyoxylate Carboligase of Escherichia coli: a Flavoprotein

3. Glyoxylate carboligase of Escherichia coli: Some properties of the enzyme

4. Escherichia coli glyoxalate carboligase. Properties and reconstitution with 5-deazaFAD and 1,5-dihydrodeazaFADH2.

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

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