Investigation of a novel liver alcohol dehydrogenase catalyzed redox-elimination reaction involving arylnitroso substrate analogues
- PMID: 6986907
- DOI: 10.1021/bi00545a019
Investigation of a novel liver alcohol dehydrogenase catalyzed redox-elimination reaction involving arylnitroso substrate analogues
Similar articles
-
Investigation of the arylnitroso reductase activity of pig liver aldehyde reductase.Biochem J. 1986 Apr 15;235(2):537-43. doi: 10.1042/bj2350537. Biochem J. 1986. PMID: 3527154 Free PMC article.
-
Rapid kinetic evidence for adduct formation between the substrate analog p-nitroso-N,N-dimethylaniline and reduced nicotinamide-adenine dinucleotide during enzymic reduction.Biochemistry. 1971 Nov 23;10(24):4569-75. doi: 10.1021/bi00800a035. Biochemistry. 1971. PMID: 4335090 No abstract available.
-
Studies on the enzymatic reduction of C-nitroso compounds. III. The kinetic analysis of C-nitrosoreductase reaction catalyzed by the cytoplasmic enzyme from porcine liver.J Biochem. 1980 Oct;88(4):1135-9. doi: 10.1093/oxfordjournals.jbchem.a133067. J Biochem. 1980. PMID: 7005209
-
The specificity of dehydrogenases.Experientia Suppl. 1980;36:85-125. doi: 10.1007/978-3-0348-5419-1_3. Experientia Suppl. 1980. PMID: 6987079 Review.
-
Methanol dehydrogenase: mechanism of action.Antonie Van Leeuwenhoek. 1989 May;56(1):25-34. doi: 10.1007/BF00822581. Antonie Van Leeuwenhoek. 1989. PMID: 2673028 Review. No abstract available.
Cited by
-
3-Hydroxylaminophenol mutase from Ralstonia eutropha JMP134 catalyzes a Bamberger rearrangement.J Bacteriol. 1999 Mar;181(5):1444-50. doi: 10.1128/JB.181.5.1444-1450.1999. J Bacteriol. 1999. PMID: 10049374 Free PMC article.
-
Investigation of the arylnitroso reductase activity of pig liver aldehyde reductase.Biochem J. 1986 Apr 15;235(2):537-43. doi: 10.1042/bj2350537. Biochem J. 1986. PMID: 3527154 Free PMC article.