Author pages are created from data sourced from our academic publisher partnerships and public sources.
- Publications
- Influence
Arginase of Bacillus brevis Nagano: purification, properties, and implication in gramicidin S biosynthesis.
- M. Kanda, K. Ohgishi, T. Hanawa, Y. Saito
- Chemistry, Medicine
- Archives of biochemistry and biophysics
- 1 August 1997
An arginase [EC 3.5.3.1] was purified to homogeneous state from a gramicidin S-producing Bacillus brevis Nagano. The enzyme has a molecular weight of about 180,000 on gel filtration. The subunit… Expand
Three conserved glycine residues in valine activation of gramicidin S synthetase 2 from Bacillus brevis.
- M. Saito, K. Hori, T. Kurotsu, M. Kanda, Y. Saito
- Biology, Medicine
- Journal of biochemistry
- 1 February 1995
The translated product from the gene fragment containing the second and third domains of gramicidin S synthetase 2 was purified to an essentially homogeneous state. It showed valine- and… Expand
Some mutants of Bacillus brevis deficient in gramicidin S formation.
- M. Iwaki, K. Shimura, M. Kanda, E. Kaji, Y. Saito
- Biology, Medicine
- Biochemical and biophysical research…
- 28 February 1974
Twenty mutants of Bacillus brevis which were deficient in gramicidin S formation were isolated by N-methyl-N′-nitrosoguanidine treatment. In addition to three groups which have been previously… Expand
Molecular cloning and nucleotide sequence of the gramicidin S synthetase 1 gene.
- K. Hori, Y. Yamamoto, +6 authors Y. Saito
- Biology, Medicine
- Journal of biochemistry
- 1 October 1989
The entire gene for gramicidin S synthetase 1 (GS 1) was cloned into the plasmid vector pUC18, and the nucleotide sequences of the GS 1 gene and its flanking region were determined. The full-length… Expand
Effect of single base substitutions at glycine-870 codon of gramicidin S synthetase 2 gene on proline activation.
- K. Tokita, K. Hori, T. Kurotsu, M. Kanda, Y. Saito
- Biology, Medicine
- Journal of biochemistry
- 1 October 1993
The mutant gene coding for a proline-activating domain (grs2-pro) was cloned and sequenced from Bacillus brevis Nagano, BII-3 strain, which produces gramicidin S synthetase 2 defective in… Expand
Purification and properties of branched chain amino acid aminotransferase from gramicidin S-producing Bacillus brevis.
- M. Kanda, K. Hori, T. Kurotsu, K. Ohgishi, T. Hanawa, Y. Saito
- Biology, Medicine
- Journal of nutritional science and vitaminology
- 1 February 1995
The branched chain amino acid aminotransferase [EC 2.6.1.42] was purified to a homogeneous state from a gramicidin S-producing strain of Bacillus brevis. The enzyme had a molecular weight of about… Expand
Studies on the dissociation of flavin adenine dinucleotide from metalloflavoproteins.
- M. Kanda, F. Brady, K. Rajagopalan, P. Handler
- Chemistry, Medicine
- The Journal of biological chemistry
- 10 February 1972
Abstract Treatment of milk xanthine oxidase and chicken liver xanthine dehydrogenase with high concentrations of salts for several hours resulted in the loss of reactivity toward O2 and NAD,… Expand
Sulfhydryl groups related to the catalytic activity of gramicidin S synthetase 1 of Bacillus brevis.
- M. Kanda, K. Hori, T. Kurotsu, S. Miura, Y. Yamada, Y. Saito
- Chemistry, Medicine
- Journal of biochemistry
- 1 July 1981
Gramicidin S synthetase 1 (GS 1) [EC 5.1.1.11] (phenylalanine racemase) of Bacillus brevis contained about six sulfhydryl groups as determined by titration of the enzyme with 5,5'-dithiobis… Expand
A comparative study of sulfhydryl groups required for the catalytic activity of gramicidin S synthetase and isoleucyl tRNA synthetase.
- M. Kanda, K. Hori, T. Kurotsu, S. Miura, Y. Saito
- Biology, Medicine
- Journal of biochemistry
- 1 September 1984
The sulfhydryl groups required for the catalytic activity of gramicidin S synthetase of Bacillus brevis and Escherichia coli isoleucyl tRNA synthetase were compared. In gramicidin S synthetase 2(GS… Expand
Electron paramagnetic resonance properties and oxidation-reduction potentials of the molybdenum, flavin, and iron-sulfur centers of chicken liver xanthine dehydrogenase.
- M. Barber, M. Coughlan, M. Kanda, K. Rajagopalan
- Chemistry, Medicine
- Archives of biochemistry and biophysics
- 1 May 1980
Abstract The oxidation-reduction potentials of the various prosthetic groups in the native and desulfo forms of chicken liver xanthine dehydrogenase, determined by potentiometric titration in 0.05 m… Expand