A new NAD+-dependent opine dehydrogenase from Arthrobacter sp. strain 1C

J Bacteriol. 1989 Aug;171(8):4466-71. doi: 10.1128/jb.171.8.4466-4471.1989.

Abstract

A new NAD+-dependent opine dehydrogenase was purified to homogeneity from Arthrobacter sp. strain 1C isolated from soil by an enrichment culture technique. The enzyme has a molecular weight of about 70,000 and consists of two identical subunits with molecular weights of about 36,000. The enzyme catalyzed a reversible oxidation-reduction reaction of opine-type secondary amine dicarboxylic acids. In the oxidative deamination reaction, the enzyme was active toward unusual opines, such as N-[1-R-(carboxyl)ethyl]-S-methionine and N-[1-R-(carboxyl)ethyl]-S-phenylalanine. In the reductive secondary amine-forming reaction with NADH as a cofactor, the enzyme utilized L-amino acids such as L-methionine, L-isoleucine, L-valine, L-phenylalanine, L-leucine, L-alanine, and L-threonine as amino donors and alpha-keto acids such as pyruvate, oxaloacetate, glyoxylate, and alpha-ketobutyrate as amino acceptors. The product enzymatically synthesized from L-phenylalanine and pyruvate in the presence of NADH was identified as N-[1-R-(carboxyl)ethyl]-S-phenylalanine.

MeSH terms

  • Amino Acids, Dicarboxylic / chemical synthesis
  • Arthrobacter / enzymology*
  • Cations
  • Chromatography, Gel
  • Chromatography, Ion Exchange
  • Kinetics
  • NAD / metabolism
  • Oxidoreductases Acting on CH-NH Group Donors / isolation & purification*
  • Oxidoreductases Acting on CH-NH Group Donors / metabolism
  • Species Specificity
  • Substrate Specificity

Substances

  • Amino Acids, Dicarboxylic
  • Cations
  • NAD
  • Oxidoreductases Acting on CH-NH Group Donors
  • opine dehydrogenase, NAD+