Abstract
Extracts of a fluorescent species of Pseudomonas grown with m-cresol, degrade gentisic acid without isomerization of the ring-fission compound, maleylpyruvate, to give eventually d-malate and pyruvate. d-Malate is also a growth substrate. l-Malate but not d-malate is oxidized by a particulate enzyme not requiring nicotinamide adenine dinucleotide (NAD) or nicotinamide adenine dinucleotide phosphate (NADP). NAD- or NADP-linked malate dehydrogenases are absent but cells contain an NADP-dependent l-malic enzyme. Exposure of cells to exogenous d-malate induces an NAD-dependent d-malic enzyme, not present when d-malate is formed endogenously. Succinate- or m-cresol-grown cells, containing no d-malic enzyme, rapidly oxidize d-malate in the presence of chloramphenicol at a concentration suffient to inhibit protein synthesis. An NADP-dependent cell-free system, prepared from succinate-grown cells which oxidized d-malate, is described.
Full text
PDFSelected References
These references are in PubMed. This may not be the complete list of references from this article.
- Chapman P. J., Hopper D. J. The bacterial metabolism of 2,4-xylenol. Biochem J. 1968 Dec;110(3):491–498. doi: 10.1042/bj1100491. [DOI] [PMC free article] [PubMed] [Google Scholar]
- FRANCIS M. J., HUGHES D. E., KORNBERG H. L., PHIZACKERLEY P. J. THE OXIDATION OF L-MALATE BY PSEUDOMONAS SP. Biochem J. 1963 Dec;89:430–438. doi: 10.1042/bj0890430. [DOI] [PMC free article] [PubMed] [Google Scholar]
- HUGHES D. E. A press for disrupting bacteria and other micro-organisms. Br J Exp Pathol. 1951 Apr;32(2):97–109. [PMC free article] [PubMed] [Google Scholar]
- Hopper D. J., Chapman P. J., Dagley S. Enzymic formation of D-malate. Biochem J. 1968 Dec;110(4):798–800. doi: 10.1042/bj1100798. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Krebs H. A., Eggleston L. V. The effect of citrate on the rotation of the molybdate complexes of malate, citramalate and isocitrate. Biochem J. 1943 Sep;37(3):334–338. doi: 10.1042/bj0370334. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LACK L. Enzymic cis-trans isomerization of maleylpyruvic acid. J Biol Chem. 1961 Nov;236:2835–2840. [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- STERN J. R. Enzymic activation and cleavage of D- and L-malate. Biochim Biophys Acta. 1963 Feb 5;69:435–438. doi: 10.1016/0006-3002(63)91288-5. [DOI] [PubMed] [Google Scholar]
- Stern J. R., O'Brien R. W. Oxidation D-malic and beta-alkylmalic acids wild-type and mutant strains of Salmonella typhimurium and by Aerobacter aerogenes. J Bacteriol. 1969 Apr;98(1):147–151. doi: 10.1128/jb.98.1.147-151.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- TUBBS P. K., GREVILLE G. D. The oxidation of D-alpha-hydroxy acids in animal tissues. Biochem J. 1961 Oct;81:104–114. doi: 10.1042/bj0810104. [DOI] [PMC free article] [PubMed] [Google Scholar]
- TUBOI S., KIKUCHI G. Enzymic cleavage of malate to glyoxylate and acetyl-coenzyme A. Biochim Biophys Acta. 1962 Jul 30;62:188–190. doi: 10.1016/0006-3002(62)90513-9. [DOI] [PubMed] [Google Scholar]
- WOLFE R. G., NEILANDS J. B. Some molecular and kinetic properties of heart malic dehydrogenase. J Biol Chem. 1956 Jul;221(1):61–69. [PubMed] [Google Scholar]