Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Purification and Characterization of Arginine Amidinohydrolase from Bacillus brevis TT02-8
Kumiko-W. ShimotohnoJunko IidaNaomi TakizawaToyoshige Endo
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JOURNAL FREE ACCESS

1994 Volume 58 Issue 6 Pages 1045-1049

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Abstract

A bacterial arginase was purified to homogeneity from a strain of Bacillus brevis. The native enzyme, with an estimated MW of 143, 000, migrated on SDS-PAGE as a single polypeptide of estimated MW of 33, 000. The enzyme, highly specific to L-arginine, showed the maximum activity at pH 11. 0 in the presence of Mn2+ ions and the pI was 4. 8 by isoelectric focusing. The enzyme activity was increased significantly by the addition of Mn2+, Ni2+, or Co2+ ions, and inhibited potently by chemicals such as HgCl2, N-bromosuccinimide, or glutathione. The Kms for L-arginine and L-canavanine were 0. 69 and 22. 2 mM, respectively. The enzyme was inhibited competitively by γ-guanidinobutyric acid, and non-competitively by L-lysine, L-ornithine, creatine, blasticidin S, and edeine B1. Analysis of the N-terminal amino acid sequence of the purified bacterial enzyme found 33-36% homologies with the Agrobacterium, yeast, rat, and human enzymes.

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