Crystal structure and reactivity of YbdL from Escherichia coli identify a methionine aminotransferase function.
Dolzan, Manuela
Crystal structure and reactivity of YbdL from Escherichia coli identify a methionine aminotransferase function. [electronic resource] - FEBS letters Jul 2004 - 141-6 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0014-5793
10.1016/j.febslet.2004.06.075 doi
Amino Acid Sequence
Base Sequence
Cloning, Molecular
Conserved Sequence
Crystallography, X-Ray
DNA Primers
Escherichia coli--enzymology
Escherichia coli Proteins--chemistry
Kinetics
Methionine--metabolism
Models, Molecular
Molecular Sequence Data
Protein Conformation
Pyridoxal Phosphate--metabolism
Recombinant Proteins--chemistry
Sensitivity and Specificity
Sequence Alignment
Sequence Homology, Amino Acid
Transaminases--chemistry
Crystal structure and reactivity of YbdL from Escherichia coli identify a methionine aminotransferase function. [electronic resource] - FEBS letters Jul 2004 - 141-6 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0014-5793
10.1016/j.febslet.2004.06.075 doi
Amino Acid Sequence
Base Sequence
Cloning, Molecular
Conserved Sequence
Crystallography, X-Ray
DNA Primers
Escherichia coli--enzymology
Escherichia coli Proteins--chemistry
Kinetics
Methionine--metabolism
Models, Molecular
Molecular Sequence Data
Protein Conformation
Pyridoxal Phosphate--metabolism
Recombinant Proteins--chemistry
Sensitivity and Specificity
Sequence Alignment
Sequence Homology, Amino Acid
Transaminases--chemistry