Abstract
Two ornithine carbamoyltransferases (OCT 1 and OCT 2) were isolated from Pseudomonas syringae pv. phaseolicola and purified by precipitation with ammonium sulfate, heat denaturation, chromatography on DEAE-Sephadex A-50 and Sephadex G-200. Molecular weights of both enzymes: 110,000; optimal activity: pH 8.5 to 9.5 (OCT 1), pH 8.4 (OCT 2); apparent K m for ornithine: 7·10-4 (both enzymes); apparent K m for carbamoylphosphate: 7·10-4 (OCT 1), 2.8·10-3 (OCT 2). Both enzymes possess only an anabolic function. OCT 1 is highly inhibited by low concentrations of phaseolotoxin and Orn-P(O)(NH2)-NH-SO3H, OCT 2 is insensitive to both compounds. The inhibition of OCT 1 is reversible.
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Abbreviations
- PNSOrn:
-
Ornithine-δ-P(O)(NH2)-NH-SO3H
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Jahn, O., Sauerstein, J. & Reuter, G. Characterization of two ornithine carbamoyltransferases from Pseudomonas syringae pv. phaseolicola, the producer of phaseolotoxin. Arch. Microbiol. 147, 174–178 (1987). https://doi.org/10.1007/BF00415280
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DOI: https://doi.org/10.1007/BF00415280