A new nicotinamide-adenine dinucleotide-dependent hydroaromatic dehydrogenase of Lactobacillus plantarum and its role in formation of (minus)t-3,t-4-dihydroxycyclohexane-c-1-carboxylate

Biochem J. 1974 Jul;141(1):35-42. doi: 10.1042/bj1410035.

Abstract

1. A new induced NAD-dependent hydroaromatic dehydrogenase was isolated from a cell-free extract of Lactobacillus plantarum 13a and purified 175-fold. 2. The enzyme catalyses the oxidation of (-)-quinate, (-)-shikimate, (-)-dihydroshikimate and (-)t-3,t-4-dihydroxycyclohexane-c-1-carboxylate with NAD(+), and the reverse action with NADH. 3. The K(m) values at the optimal pH10.0 for these substrates are 0.85, 0.75, 0.52 and 0.74mm respectively, and the corresponding values for NAD(+) are 0.45, 0.26, 0.34 and 0.36mm respectively. 4. The stereochemical requirements of the enzyme and the role it may play in the reduction of (-)-quinate to (-)t-3,t-4-dihydroxycyclohexane-c-1-carboxylate are discussed and a pathway is suggested.

MeSH terms

  • Centrifugation
  • Chemical Precipitation
  • Chromatography, DEAE-Cellulose
  • Chromatography, Gel
  • Chromatography, Paper
  • Cyclohexanecarboxylic Acids / biosynthesis*
  • Hydro-Lyases
  • Hydrogen-Ion Concentration
  • Kinetics
  • Lactobacillus / enzymology*
  • NAD*
  • Oxidoreductases*
  • Quinic Acid / metabolism
  • Shikimic Acid / metabolism
  • Spectrophotometry, Ultraviolet

Substances

  • Cyclohexanecarboxylic Acids
  • Quinic Acid
  • NAD
  • Shikimic Acid
  • Oxidoreductases
  • Hydro-Lyases