Structural Insight into Substrate Binding and Catalysis of a Novel 2-Keto-3-deoxy-d-arabinonate Dehydratase Illustrates Common Mechanistic Features of the FAH Superfamily-Reference-Cited by-同舟云学术

Structural Insight into Substrate Binding and Catalysis of a Novel 2-Keto-3-deoxy-d-arabinonate Dehydratase Illustrates Common Mechanistic Features of the FAH Superfamily

Published:2008-05 Issue:2 Volume:379 Page:357-371
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Brouns Stan J.J.,Barends Thomas R.M.,Worm Petra,Akerboom Jasper,Turnbull Andrew P.,Salmon Laurent,van der Oost John

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

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3. Identification and characterization of L-arabonate dehydratase, L-2-keto-3-deoxyarabonate dehydratase, and L-arabinolactonase involved in an alternative pathway of L-arabinose metabolism. Novel evolutionary insight into sugar metabolism;Watanabe;J. Biol. Chem.,2006

4. A novel alpha-ketoglutaric semialdehyde dehydrogenase: evolutionary insight into an alternative pathway of bacterial L-arabinose metabolism;Watanabe;J. Biol. Chem.,2006

5. Genetic analysis of a novel pathway for D-xylose metabolism in Caulobacter crescentus;Stephens;J. Bacteriol.,2007

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