Physical and chemical evidence for the trimeric subunit structure of 2-keto-4-hydroxyglutarate aldolase from Escherichia coli K-12.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference43 articles.
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5. Purification, Substrate Specificity and Binding, β-Decarboxylase Activity, and Other Properties of Escherichia coli 2-Keto-4-hydroxyglutarate Aldolase
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1. Immobilization of Enzymes: An Approach to Fundamental Studies in Biochemistry;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22
2. Covalent intermediate trapped in 2-keto-3-deoxy-6- phosphogluconate (KDPG) aldolase structure at 1.95-A resolution;Proceedings of the National Academy of Sciences;2001-03-27
3. Aldolases;Comprehensive Natural Products Chemistry;1999
4. Purification and properties of 2'-hydroxybenzalpyruvate aldolase from a bacterium that degrades naphthalenesulfonates;Journal of Biological Chemistry;1993-05
5. 2-Keto-4-hydroxyglutarate aldolase: purification and characterization of the homogeneous enzyme from bovine kidney.;Journal of Biological Chemistry;1992-05
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