1972
DOI: 10.1104/pp.49.5.808
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Mode of Action of the Toxin from Pseudomonas phaseolicola

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

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Cited by 39 publications
(14 citation statements)
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“…The apple leaf enzyme seems to have binding constants very similar to those reported for the enzyme in other systems (9,14). At both pH optima, the enzyme(s) is better able to bind C-P than ORN.…”
Section: Resultssupporting
confidence: 60%
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“…The apple leaf enzyme seems to have binding constants very similar to those reported for the enzyme in other systems (9,14). At both pH optima, the enzyme(s) is better able to bind C-P than ORN.…”
Section: Resultssupporting
confidence: 60%
“…At both pH optima, the enzyme(s) is better able to bind C-P than ORN. In this respect, this enzyme is similar to the one found in bacterial systems (9), but differs from the one found in the bean plant (14). The pH 8.6 enzyme has slightly higher affinities for ORN and C-P than does the pH 7.8 enzyme.…”
Section: Resultssupporting
confidence: 51%
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“…It produces phaseolotoxin, a tripeptide consisting of homoarginine, alanine and ornithine which is substituted in its b-aminogroup, om-P(0) (NHJ-NH-S0,H. Furthermore it produces this substituted ornithine (PNSOrn) 1977, PATIL et al 1970, TAM and PATIL 1972. Searching for the molecular basis of the resistance of P. phaseolicola against the selfproduced toxin we found a second OCT, which is insensitive to the toxin (JAHN el at.…”
mentioning
confidence: 97%