The high-resolution structure of dihydrodipicolinate synthase from Escherichia coli bound to its first substrate, pyruvate.
Devenish, Sean R A
The high-resolution structure of dihydrodipicolinate synthase from Escherichia coli bound to its first substrate, pyruvate. [electronic resource] - Acta crystallographica. Section F, Structural biology and crystallization communications Dec 2008 - 1092-5 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
1744-3091
10.1107/S1744309108033654 doi
Binding Sites
Crystallography, X-Ray
Databases, Protein
Escherichia coli--enzymology
Escherichia coli Proteins--chemistry
Hydro-Lyases--chemistry
Kinetics
Oxaloacetic Acid--metabolism
Pyruvic Acid--metabolism
Substrate Specificity
The high-resolution structure of dihydrodipicolinate synthase from Escherichia coli bound to its first substrate, pyruvate. [electronic resource] - Acta crystallographica. Section F, Structural biology and crystallization communications Dec 2008 - 1092-5 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
1744-3091
10.1107/S1744309108033654 doi
Binding Sites
Crystallography, X-Ray
Databases, Protein
Escherichia coli--enzymology
Escherichia coli Proteins--chemistry
Hydro-Lyases--chemistry
Kinetics
Oxaloacetic Acid--metabolism
Pyruvic Acid--metabolism
Substrate Specificity