The microbial oxidation of methanol. The prosthetic group of the alcohol dehydrogenase of Pseudomonas sp. M27: a new oxidoreductase prosthetic group
- PMID: 6049934
- PMCID: PMC1271238
- DOI: 10.1042/bj1040960
The microbial oxidation of methanol. The prosthetic group of the alcohol dehydrogenase of Pseudomonas sp. M27: a new oxidoreductase prosthetic group
Abstract
1. The purified alcohol dehydrogenase of Pseudomonas sp. M27, whose action is independent of nicotinamide nucleotides, has absorption peaks at 280mmu and at 350mmu with little or no absorption at or above 450mmu. 2. It does not fluoresce, but green-fluorescent material, diffusible on dialysis, is produced when the enzyme is treated with acid or alkali or when it is boiled. 3. Evidence is presented that the enzyme is not a flavoprotein. 4. Kinetic studies show a correlation between enzyme inactivation by acid, alkali or heat and liberation of the fluorescent material. 5. Some purification of the fluorescent material was achieved, but definite identification was not possible; the major component has a fluorescence maximum at about 460mmu with excitation maxima at about 260mmu and 365mmu. 6. Data are given (including absorption and fluorescence spectra) that support the suggestion that the prosthetic group of the enzyme is a pteridine derivative. 7. Possible mechanisms of action of the enzyme are discussed.
Similar articles
-
The microbial oxidation of methanol. Purification and properties of the alcohol dehydrogenase of Pseudomonas sp. M27.Biochem J. 1967 Sep;104(3):953-9. doi: 10.1042/bj1040953. Biochem J. 1967. PMID: 6058112 Free PMC article.
-
Microbial oxidation of amines. Spectral and kinetic properties of the primary amine dehydrogenase of Pseudomonas AM1.Biochem J. 1971 Aug;123(5):757-71. doi: 10.1042/bj1230757. Biochem J. 1971. PMID: 5124384 Free PMC article.
-
The microbial oxidation of methanol. The alcohol dehydrogenase of Pseudomonas sp. M27.Biochem J. 1965 Sep;96(3):808-12. doi: 10.1042/bj0960808. Biochem J. 1965. PMID: 5862419 Free PMC article.
-
Physiological studies of methane- and methanol-oxidizing bacteria: comparison of a primary alcohol dehydrogenase from Methylococcus capsulatus (Texas strain) and Pseudomonas species M27.J Bacteriol. 1972 May;110(2):570-7. doi: 10.1128/jb.110.2.570-577.1972. J Bacteriol. 1972. PMID: 5022170 Free PMC article.
-
Fluorescent pigments in the newly isolated methylotrophs: Pseudomonas J16 and Methylomonas Pl1.Acta Microbiol Pol. 1978;27(3):257-67. Acta Microbiol Pol. 1978. PMID: 81599
Cited by
-
(1-14C) acetate assimilation by obligate methylotrophs, Pseudomonas methanica and Methylosinus trichosporium.Antonie Van Leeuwenhoek. 1979;45(3):499-511. doi: 10.1007/BF00443287. Antonie Van Leeuwenhoek. 1979. PMID: 122051
-
Metabolic characteristics of an aerobe isolated from a methylotrophic methanogenic enrichment culture.J Biosci. 2003 Mar;28(2):235-42. doi: 10.1007/BF02706223. J Biosci. 2003. PMID: 12711816
-
The interaction between methanol dehydrogenase and the autoreducible cytochromes c of the facultative methylotroph Pseudomonas AM1.Biochem J. 1980 Aug 15;190(2):481-4. doi: 10.1042/bj1900481. Biochem J. 1980. PMID: 6258570 Free PMC article.
-
The prosthetic group of methanol dehydrogenase. Purification and some of its properties.Biochem J. 1980 Apr 1;187(1):221-6. doi: 10.1042/bj1870221. Biochem J. 1980. PMID: 6996672 Free PMC article.
-
The mtrAB operon of Bacillus subtilis encodes GTP cyclohydrolase I (MtrA), an enzyme involved in folic acid biosynthesis, and MtrB, a regulator of tryptophan biosynthesis.J Bacteriol. 1992 Apr;174(7):2059-64. doi: 10.1128/jb.174.7.2059-2064.1992. J Bacteriol. 1992. PMID: 1551827 Free PMC article.
References
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources