Health & Environmental Research Online (HERO)


Print Feedback Export to File
8685567 
Journal Article 
Enzymic aromatization of 3,5-cyclohexadiene-1,2-diol 
Ayengar, PK; Hayaishi, O; Nakajima, M; Tomida, I 
1959 
1 
Biochimica et Biophysica Acta
ISSN: 0006-3002
EISSN: 1878-2434 
33 
1 
111-119 
English 
1. 1. 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. 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. 3. The optimum pH of the reaction was found to be 9.0. Michaelis constants were 2.4·10-4 M for TPN and 7.05·10-3 M for DIOL. 4. 4. All attempts to reverse the reaction proved unseccessful. 5. 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. 1959.