ISSN:
1617-4623
Keywords:
Ornithine carbamoyltransferase
;
Phaseolotoxin tolerance
;
Pseudomonas syringae pv.phaseolicola
;
Nucleotide sequence
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Summary The gene coding for the phaseolotoxin-insensitive ornithine carbamoyltransferase (OCTase) fromPseudomonas syringae pv.phaseolicola has been cloned and sequenced. The gene has a deduced coding capacity for a polypeptide with a calculated M, of 36520 daltons. Comparison of the amino acid sequence of the OCTase enzymes encoded by theP. aeruginosa argF and theEscherichia coli argI andargF genes with the deduced sequence of the newly identified gene shows that 79 amino acid residues are strictly conserved in all four polypeptides; among these 7 out of 9 residues are involved in enzyme function. Of three amino acid regions that have been implicated in substrate binding or catalysis, two are strictly conserved, and the third involved in carbamoylphosphate binding differs. This correlates well with published data showing that phaseolotoxin competes for the carbamoylphosphate binding site in the phaseolotoxin-sensitive OCTases. We propose that the gene be namedargK.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00633857
Permalink