A Novel NADP+-dependent Serine Dehydrogenase fromAgrobacterium tumefaciens
- 1 January 1997
- journal article
- Published by Taylor & Francis in Bioscience, Biotechnology, and Biochemistry
- Vol. 61 (1) , 152-157
- https://doi.org/10.1271/bbb.61.152
Abstract
NADP+-dependent serine dehydrogenase [EC 1.1.1.–], which catalyzes the oxidation of the hydroxyl group of serine to form 2-aminomalonate semialdehyde, was purified to homogeneity from a crude extract of Agrobacterium tumefaciens ICR 1600. The enzyme had a molecular mass of about 100 kDa and consisted of four identical subunits. In addition to l-serine, d-serine, l-glycerate, d-glycerate, and 2-methyl-dl-serine were substrates. However, O-methyl-dl-serine and l-threonine were inert. The enzyme showed maximal activity at about pH 9 for the oxidation of l-serine. The enzyme required NADP+ as a coenzyme, NAD + was inert. The enzyme was not inhibited by EDTA, o-phenanthroline, or α, α′-dipyridyl, but was inhibited by HgCl2, p-chloromercuribenzoate, l-cysteine, d-cysteine, malonate, 2-methylmalonate, and tartronate. The Michaelis constants for l-serine, d-serine, and NADP+ were 42, 44, and 0.029 mm, respectively.Keywords
This publication has 1 reference indexed in Scilit:
- 5 Glutamate DehydrogenasesPublished by Elsevier ,1975