Glycine, serine and threonine metabolism
Studies on the catalytic and regulatory properties of homoserine dehydrogenase of Zea mays roots.
Effects of K+ on the catalytic and regulatory properties of homoserine dehydrogenase of Pseudomonas fluorescens.
The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K12. The two catalytic activities are carried by two independent regions of the polypeptide chain.
The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli K 12. Intra and intersubunit interactions between the catalytic regions of the bifunctional enzyme.
Cobalt(III) affinity-labeled aspartokinase. Formation of substrate and inhibitor adducts.
Homoserine dehydrogenase of Rhodospirillum rubrum. Physical and chemical characterization.
Sequential folding of a bifunctional allosteric protein.
The interaction between Escherichia coli aspartokinase-homoserine dehydrogenase and 3-acetylpyridine-adenine dinucleotide phosphate (reduced), an analog of NADPH.
The kinetic mechanisms of the bifunctional enzyme aspartokinase-homoserine dehydrogenase I from Escherichia coli.
Role of serine 352 in the allosteric response of Serratia marcescens aspartokinase I-homoserine dehydrogenase I analyzed by using site-directed mutagenesis.
Crystallization and preliminary X-ray diffraction studies of homoserine dehydrogenase from Saccharomyces cerevisiae.
Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductases.
Homoserine dehydrogenase from Saccharomyces cerevisiae: kinetic mechanism and stereochemistry of hydride transfer.
Characterization of yeast homoserine dehydrogenase, an antifungal target: the invariant histidine 309 is important for enzyme integrity.
Production and characterization of bifunctional enzymes. Domain swapping to produce new bifunctional enzymes in the aspartate pathway.
Enzyme-assisted suicide: molecular basis for the antifungal activity of 5-hydroxy-4-oxonorvaline by potent inhibition of homoserine dehydrogenase.
New phenolic inhibitors of yeast homoserine dehydrogenase.