Synthesis of L-arabinose isomerase (L-arabinose ketol isomerase, EC 5. 3. 1. 4) was studied in the wild-type and mutant strains of
Vibrio parahaemolyticus. Two mutant strains, 2001 and 2126, used in this study were described previously (Iuchi et al.: J. Bacteriol. 124, 567-569, 1975). Strain 2001 is probably equivalent to the
crp mutant lacking cyclic adenosine 3', 5'-monophosphate (cyclic AMP) receptor protein (CRP) of
Escherichia coli. Strain 2126 is phenotypically similar to the
cya mutant of E. coli deficient in adenylate cyclase, but the exact nature of this mutant is yet unknown.
L-Arabinose isomerase of
V. parahaemolyticus was an inducible enzyme, and its activity was detected only when L-arabinose was present in the medium. The enzyme synthesis in the mutants was greatly impaired, and the specific activity obtained with each mutant was about 30% of that obtained with the wild-type strain. Cyclic AMP added to the medium could restore L-arabinose isomerase synthesis in strain 2126, indicating that the nucleotide, as well as the inducer L-arabinose, was required for synthesis of the enzyme. Glucose and galactose present in the medium repressed the enzyme synthesis of the wild-type strain by about 90 and 55%, respectively. No repression was observed with glycerol. All these findings suggest that Larabinose isomerase of
V. parahaemolyticus is a typical catabolic enzyme, whose synthesis is regulated in the same manner as that of various catabolic enzymes of
E. coli.
View full abstract