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 Km for ornithine: 7 X 10(-4) (both enzymes); apparent Km for carbamoyl-phosphate: 7 X 10(-4) (OCT 1), 2.8 X 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.
journal_name
Arch Microbioljournal_title
Archives of microbiologyauthors
Jahn O,Sauerstein J,Reuter Gdoi
10.1007/BF00415280subject
Has Abstractpub_date
1987-03-01 00:00:00pages
174-8issue
2eissn
0302-8933issn
1432-072Xjournal_volume
147pub_type
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