Abstract
Growth of Acinetobacter calcoaceticus strain BD413 in malate-mineral medium resulted in the excretion of large quantities of oxalacetate. Malate was virtually depleted by the time the cell density reached 60% of its final value; most of the remaining growth took place at the expense of oxalacetate. Experiments in which oxalacetate was used as the initial substrate showed that pyruvate was not utilized until most of the oxalacetate disappeared. The generation time for growth on malate or oxalacetate was ∼40 min; the generation time for growth on pyruvate was 62 min, which implies that pyruvate transport may be rate limiting. Oxalacetate and pyruvate, however, supported approximately the same growth yield. These observations suggested that the first step in the utilization of oxalacetate as an energy source consisted of an enzymatic decarboxylation of the keto acid to pyruvate and CO2. Three enzyme reactions that carry out this decarboxylation have been detected in extracts of A. calcoaceticus. The first, which functioned maximally at pH 4.8, was attributable to the oxalacetate decarboxylase activity of oxidized diphosphopyridine nucleotide-malic enzyme. The second and third, which functioned in the neutral pH range, resulted from coupling of oxidized diphosphopyridine nucleotide-malic enzyme to reduced diphosphopyridine nucleotide-dependent malic dehydrogenase, and oxidized triphosphopyridine nucleotide-malic enzyme to a reduced triphosphopyridine nucleotide-dependent malic dehydrogenase. The efficiency of these coupled reactions was high enough so that the overall reaction could be physiologically significant.
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- Dolin M. I. Kinetics of malic-lactic transhydrogenase. Abortive complex formation with substrates and products. J Biol Chem. 1969 Oct 10;244(19):5273–5285. [PubMed] [Google Scholar]
- Dolin M. I. Kinetics of malic-lactic transhydrogenase. Effect of the keto-enol tautomerism of oxalacetate on the kinetics of oxalacetate formation and utilization. J Biol Chem. 1968 Jul 25;243(14):3916–3923. [PubMed] [Google Scholar]
- Hatch M. D., Mau S. L., Kagawa T. Properties of leaf NAD malic enzyme from plants with C4 pathway photosynthesis. Arch Biochem Biophys. 1974 Nov;165(1):188–200. doi: 10.1016/0003-9861(74)90155-6. [DOI] [PubMed] [Google Scholar]
- Herman N. J., Bell E. J. Metabolic control in Acinetobacter sp. I. Effect of C4 versus C2 and C3 substrates on isocitrate lyase synthesis. Can J Microbiol. 1970 Aug;16(8):769–774. doi: 10.1139/m70-130. [DOI] [PubMed] [Google Scholar]
- Hernandez E., Johnson M. J. Energy supply and cell yield in aerobically growth microorganisms. J Bacteriol. 1967 Oct;94(4):996–1001. doi: 10.1128/jb.94.4.996-1001.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Juni E., Janik A. Transformation of Acinetobacter calco-aceticus (Bacterium anitratum). J Bacteriol. 1969 Apr;98(1):281–288. doi: 10.1128/jb.98.1.281-288.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kleber H. P., Aurich H. Regulation der Aktivität des Malatenzyms aus Acinetobacter durch organische Säuren. Z Allg Mikrobiol. 1976;16(2):91–95. doi: 10.1002/jobm.3630160202. [DOI] [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]
- Lin R. C., Davis E. J. Malic enzymes of rabbit heart mitochondria. Separation and comparison of some characteristics of a nicotinamide adenine dinucleotide-preferring and a nicotinamide adenine dinucleotide phosphate-specific enzyme. J Biol Chem. 1974 Jun 25;249(12):3867–3875. [PubMed] [Google Scholar]
- Pertierra A. G., Cooper R. A. Pyruvate formation during the catabolism of simple hexose sugars by Escherichia coli: studies with pyruvate kinase-negative mutants. J Bacteriol. 1977 Mar;129(3):1208–1214. doi: 10.1128/jb.129.3.1208-1214.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- RUTTER W. J., LARDY H. A. Purification and properties of pigeon liver malic enzyme. J Biol Chem. 1958 Aug;233(2):374–382. [PubMed] [Google Scholar]
- Reeves R. E. Phosphopyruvate carboxylase from entamoeba histolytica. Biochim Biophys Acta. 1970 Nov 11;220(2):346–349. doi: 10.1016/0005-2744(70)90021-5. [DOI] [PubMed] [Google Scholar]
- Sanwal B. D., Smando R. Malic enzyme of Escherichia coli. Diversity of the effectors controlling enzyme activity. J Biol Chem. 1969 Apr 10;244(7):1817–1823. [PubMed] [Google Scholar]
- Saz H. J., Lescure O. L. The functions of phosphoenolpyruvate carboxykinase and malic enzyme in the anaerobic formation of succinate by Ascaris lumbricoides. Comp Biochem Physiol. 1969 Jul 1;30(1):49–60. doi: 10.1016/0010-406x(69)91296-1. [DOI] [PubMed] [Google Scholar]
- Stern J. R. Oxalacetate decarboxylase of Aerobacter aerogenes. I. Inhibition by avidin and requirement for sodium ion. Biochemistry. 1967 Nov;6(11):3545–3551. doi: 10.1021/bi00863a028. [DOI] [PubMed] [Google Scholar]
- TAYLOR W. H., JUNI E. Pathways for biosynthesis of a bacterial capsular polysaccharide. I. Carbohydrate metabolism and terminal oxidation mechanisms of a capsuleproducing coccus. J Bacteriol. 1961 May;81:694–703. doi: 10.1128/jb.81.5.694-703.1961. [DOI] [PMC free article] [PubMed] [Google Scholar]
- YOUNG J. W., SHRAGO E., LARDY H. A. METABOLIC CONTROL OF ENZYMES INVOLVED IN LIPOGENESIS AND GLUCONEOGENESIS. Biochemistry. 1964 Nov;3:1687–1692. doi: 10.1021/bi00899a015. [DOI] [PubMed] [Google Scholar]
- Yamaguchi M., Tokushige M., Katsuki H. Studies on regulatory functions of malic enzymes. II. Purification and molecular properties of nicotinamide adenine dinucleotide-linked malic enzyme from Eschericha coli. J Biochem. 1973 Jan;73(1):169–180. [PubMed] [Google Scholar]