(PDF) 2-Amino-3-Ketobutyrate CoA Ligase of Escherichia

2-Amino-3-Ketobutyrate CoA Ligase of Escherichia Coli: Stoichiometry of Pyridoxal Phosphate Binding and Location of the Pyridoxyllysine Peptide in the Primary Structure of the Enzyme

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

doi 10.1016/0167-4838(90)90097-y

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Date

January 1, 1990

Authors

Jagat J. Mukherjee

Eugene E. Dekker

Publisher

Elsevier BV

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2-Amino-3-Ketobutyrate CoA Ligase of Escherichia Coli: Stoichiometry of Pyridoxal Phosphate Binding and Location of the Pyridoxyllysine Peptide in the Primary Structure of the Enzyme

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

doi 10.1016/0167-4838(90)90097-y

Full Text

Abstract

Date

Authors

Publisher

Related search

Nucleotide Sequence of the 2-Amino-3-Ketobutyrate Coenzyme a Ligase (Kbl) Gene ofE.coli

Conserved Pyridoxal 5′-Phosphate Binding Protein YggS Impacts Amino Acid Metabolism Through Pyridoxine 5′-Phosphate in Escherichia Coli

Crystal Structure of Pyridoxal Kinase From the Escherichia Coli pdxK Gene: Implications for the Classification of Pyridoxal Kinases

Control of the Synthesis of Alkaline Phosphatase and the Phosphate-Binding Protein in Escherichia Coli.

2-Keto-3-Deoxygluconate 6-Phosphate Aldolase Mutants of Escherichia Coli

The NMR Structure of the 47-kDa Dimeric Enzyme 3,4-Dihydroxy-2-Butanone-4-Phosphate Synthase and Ligand Binding Studies Reveal the Location of the Active Site

Substrate Attachment in Enzymes. The Interaction of Pyridoxal Phosphate With Amino Acids

Physical Map Location of the Peptide Methionine Sulfoxide Reductase Gene on the Escherichia Coli Chromosome.

The Binding of Pyridoxal 5-Phosphate to Aspartate Aminotransferase of Pig Heart