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Tam LQ, Patil SS. Mode of Action of the Toxin from Pseudomonas phaseolicola: II. Mechanism of Inhibition of Bean Ornithine Carbamoyltransferase. Plant Physiol. 1972;49(5):808-12doi: 10.1104/pp.49.5.808.
Tam, L. Q., & Patil, S. S. (1972). Mode of Action of the Toxin from Pseudomonas phaseolicola: II. Mechanism of Inhibition of Bean Ornithine Carbamoyltransferase. Plant physiology, 49(5), 808-12. https://doi.org/10.1104/pp.49.5.808
Tam, L Q, and Patil, S S. "Mode of Action of the Toxin from Pseudomonas phaseolicola: II. Mechanism of Inhibition of Bean Ornithine Carbamoyltransferase." Plant physiology vol. 49,5 (1972): 808-12. doi: https://doi.org/10.1104/pp.49.5.808
Tam LQ, Patil SS. Mode of Action of the Toxin from Pseudomonas phaseolicola: II. Mechanism of Inhibition of Bean Ornithine Carbamoyltransferase. Plant Physiol. 1972 May;49(5):808-12. doi: 10.1104/pp.49.5.808. PMID: 16658053; PMCID: PMC366057.
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Plant Physiol. 1972 May;49(5):808-12. doi: 10.1104/pp.49.5.808.

Mode of Action of the Toxin from Pseudomonas phaseolicola: II. Mechanism of Inhibition of Bean Ornithine Carbamoyltransferase.

Plant physiology

L Q Tam, S S Patil

Affiliations

  1. Department of Plant Pathology, University of Hawaii, 3190 Maile Way, Honolulu, Hawaii 96822.

PMID: 16658053 PMCID: PMC366057 DOI: 10.1104/pp.49.5.808

Abstract

A chlorosis-inducing toxin of Pseudomonas phaseolicola was examined for inhibition of ornithine carbamoyltransferease prepared from acetone powder of bean (Phaseolus vulgaris L.) plants. The enzyme has a pH optimum at 8.5, involves a ternary complex reaction mechanism, and shows Michaelis constants of 5.0 mm and 1.7 mm for ornithine and carbamoylphosphate, respectively. Assuming reversible catalysis, Michaelas constants of 11 mm and 3.3 mm are calculated for citrulline and arsenate. Toxin induces allosteric competitive inhibition in relation to carbamoylphosphate and a noncompetitive mode of inhibition in relation to ornithine, except at high toxin concentrations where uncompetitive inhibition is observed. In the backward assay, competitive inhibition is observed for both arsenate and citrulline. Inhibition is increased with preincubation time and shows saturation kinetics with regard to toxin concentration.

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