Trypotophanase from a marine bacterium, Vibrio K-7 synthesis, purification and some chemical catalytic properties

Archives of Microbiology
D D WhittR D DeMoss

Abstract

The conditions for synthesis, purification, and properties of tryptophanase by a marine organism (Vibrio K-7) were studied. Tryptophanase was induced by tryptophan and its analogs, and partially repressed by 0.5% glucose or glycerol. NaCl (0.4 M) was required for optimal growth and tryptophanase activity in whole cells. The enzyme was purified to 92% homogeneity by heat treatment, hydroxyapatite chromatography and fractionation with ammonium sulfate. This tryptophanase has been found to have kinetic properties similar to the tryptophanase from other microorganisms. It carries out both alpha, beta-elimination reactions (using tryptophan, serine, cysteine and S-methylcysteine as substrates) and beta-replacement reactions (forming tryptophan from indole and serine, cysteine or S-methyl-cysteine). The enzyme has a sedimentation coefficient of 9.2S and requires pyridoxal 5'-phosphate as a cofactor. The optimal pH for the tryptophanase reaction is pH 8.0.

References

Apr 1, 1973·Journal of Bacteriology·S O Hoch, R D DeMoss
Apr 1, 1971·Journal of Bacteriology·M J Klug, R D DeMoss
Mar 1, 1970·Journal of Bacteriology·S K Griffiths, R D DeMoss
Apr 1, 1969·Journal of Bacteriology·R D DeMoss, K Moser
Apr 29, 1961·Biochimica Et Biophysica Acta·A B PARDEE, L S PRESTIDGE
Mar 1, 1964·Proceedings of the National Academy of Sciences of the United States of America·W A NEWTON, E E SNELL

Citations

Jan 15, 2010·FEMS Microbiology Reviews·Jin-Hyung Lee, Jintae Lee

Related Concepts

Metazoa
Uca
Enzyme Induction
Enzyme Repression
Hydrogen-Ion Concentration
Desmolases
Seawater
Sodium Chloride, (24)NaCl
Substrate Specificity
Tryptophanase

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