A new nicotinamide–adenine dinucleotide-dependent hydroaromatic dehydrogenase of Lactobacillus plantarum and its role in formation of (-)t-3t-4-dihydroxycyclohexane-c-1-carboxylate
Keyword(s):
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 Km 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.
1967 ◽
Vol 25
◽
pp. 78-79
1964 ◽
Vol 88
(3)
◽
pp. 461-465
Keyword(s):
1972 ◽
Vol 3
(17)
◽
pp. 607-612
◽
2020 ◽
Vol 11
(4)
◽
pp. 6526-6531
1985 ◽
Vol 75
(5)
◽
pp. 1740-1743
◽
1967 ◽
Vol 28
(2)
◽
pp. 213-224
◽