Characterization of two ornithine carbamoyltransferases from Pseudomonas syringae pv. phaseolicola, the producer of phaseolotoxin.

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 Microbiol

journal_title

Archives of microbiology

authors

Jahn O,Sauerstein J,Reuter G

doi

10.1007/BF00415280

subject

Has Abstract

pub_date

1987-03-01 00:00:00

pages

174-8

issue

2

eissn

0302-8933

issn

1432-072X

journal_volume

147

pub_type

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