Purification to homogeneity and characterization of homoserine kinase from wheat germ
1993
Riesmeier, J. | Klonus, A.K. | Pohlenz, H.D.
Homoserine kinase (EC 2.7.1.39) has been purified from wheat germ to homogeneity. The native Mr of the enzyme was estimated by gel filtration to be 75000. The enzyme seems to be a homodimer with a subunit Mr of 36000. No evidence was obtained for the existence of isoforms of the enzyme. The apparent Km values were determined to be 0.24 mM for homoserine and 0.33 mM for ATP. The enzyme activity was not significantly influenced by any of the aspartate-derived amino acids (threonine, methionine, isoleucine, lysine) at least at physiologically relevant concentrations, nor by L-S-adenosylmethionine which is known to be a regulatory metabolite of the pathway.
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