Abstract
Homoserine kinase (EC 2.7.1.39) has been purified from wheat germ to homogeneity. The native M r of the enzyme was estimated by gel filtration to be 75 000. The enzyme seems to be a homodimer with a subunit M r of 36 000. No evidence was obtained for the existence of isoforms of the enzyme. The apparent K m 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 metabolise of the pathway.
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