Enzymic aromatization of 3,5-cyclohexadiene-1,2-diol
1959; Elsevier BV; Volume: 33; Issue: 1 Linguagem: Inglês
10.1016/0006-3002(59)90504-9
ISSN1878-2434
AutoresPadmadini K. Ayengar, Osamu Hayaishi, Minoru Nakajima, Ichiro Tomida,
Tópico(s)Algal biology and biofuel production
Resumo1. Extracts of rabbit-liver acetone powder have seen shown to catalyze the formation of catechol from 3,5-cyclohexadiene-1,2-diol. TPN is required for this dehydrogenation reaction. 2. The mammalian enyme oxidized DIOL and naphtalene,1,2-dihydro-1,2-diol, but had no effect on d-quinic acid, myo-inositol, 2,3-butanediol, glycerol, l-gulonic and galactonic acids. 3. The optimum pH of the reaction was found to be 9.0. Michaelis constants were 2.4·10−4M for TPN and 7.05·10−3M for DIOL. 4. All attempts to reverse the reaction proved unseccessful. 5.Diol-dehydrogenase activity was also observed in crude extracts of Aerobacter aerogenes. However, the bacterial enzyme required DPN for maximal activity and did not oxidize naphthalene-dihydro-diol.
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