A new antitumor enzyme, L-lysine alpha-oxidase from Trichoderma viride. Purification and enzymological properties.
- H. Kusakabe, K. Kodama, A. Kuninaka, H. Yoshino, H. Misono, K. Soda
- Biology, ChemistryJournal of Biological Chemistry
- 10 February 1980
L-Lysine alpha-oxidase from Trichoderma viride Y244-2 has been purified to homogeneity and several lysine analogs such as delta-hydroxylysine are oxidized efficiently.
Differences in effects on DNA gyrase activity between two glutamate racemases of Bacillus subtilis, the poly-gamma-glutamate synthesis-linking Glr enzyme and the YrpC (MurI) isozyme.
- M. Ashiuchi, Eriko Kuwana, K. Komatsu, K. Soda, H. Misono
- BiologyFEMS Microbiology Letters
- 1 June 2003
Physiological and biochemical characteristics of poly gamma-glutamate synthetase complex of Bacillus subtilis.
- M. Ashiuchi, C. Nawa, H. Misono
- Biology, ChemistryEuropean Journal of Biochemistry
- 15 October 2001
The gene-disruption experiment showed that the enzymatic system was the sole machinery of PGA synthesis in B. subtilis, and the PGA synthetase complex, PgsBCA, was suggested to be an atypical amide ligase.
The GLY1 gene of Saccharomyces cerevisiae encodes a low-specific L-threonine aldolase that catalyzes cleavage of L-allo-threonine and L-threonine to glycine--expression of the gene in Escherichia…
- J. Liu, S. Nagata, T. Dairi, H. Misono, S. Shimizu, H. Yamada
- Biology, ChemistryEuropean Journal of Biochemistry
- 1 April 1997
The GLY1 gene was amplified by PCR, with a designed ribosome-binding site, cloned into pUC118, and expressed in Escherichia coli cells, and the enzyme was purified to homogeneity, as judged by polyacrylamide gel electrophoresis.
A Poly-γ-glutamate Synthetic System of Bacillus subtilis IFO 3336: Gene Cloning and Biochemical Analysis of Poly-γ-glutamate Produced by Escherichia coli Clone Cells
- M. Ashiuchi, K. Soda, H. Misono
- Biology
- 16 September 1999
Three genes encoding a poly-gamma-glutamate synthetic system of Bacillus subtilis IFO 3336 (Bacillus natto) were cloned and expressed in Escherichia coli, resulting in a higher polymer yield and co-expression of glutamate racemase gene in E. coli cells harboring pgsBCA genes increased both the polymer production and D-glUTamate content in the polymer.
Enzymatic Synthesis of High-Molecular-Mass Poly-γ-Glutamate and Regulation of Its Stereochemistry
- M. Ashiuchi, Kazuya Shimanouchi, H. Misono
- Chemistry, BiologyApplied and Environmental Microbiology
- 1 July 2004
The results suggest that the stereochemical properties of enzymatically synthesized PGAs substantially depend on the stereochemistry of glutamate as the substrate, and genetic analysis indicated that all the pgsB, -C, and -A gene products were also indispensable for enzymatic PGA synthesis.
Properties of glutamate racemase from Bacillus subtilis IFO 3336 producing poly-gamma-glutamate.
- M. Ashiuchi, K. Tani, K. Soda, H. Misono
- Biology, ChemistryJournal of Biochemistry (Tokyo)
- 1998
The results suggest that the glutamate racemase is mainly concerned in D-glutamate synthesis for poly-gamma- glutamate production in B. subtilis IFO 3336.
Isolation of Bacillus subtilis (chungkookjang), a poly-γ-glutamate producer with high genetic competence
- M. Ashiuchi, T. Kamei, H. Misono
- BiologyApplied Microbiology and Biotechnology
- 1 December 2001
During PGA production, glutamate racemase activity was found in the cells, suggesting that the enzyme is involved in the D-glutamate supply, and B. subtilis (chungkookjang) harbors no plasmid and is the first B.subtilis strain reported with both naturally high PGA productivity and high genetic competence.
Meso-alpha,epsilon-diaminopimelate D-dehydrogenase: distribution and the reaction product
- H. Misono, H. Togawa, T. Yamamoto, K. Soda
- Biology, ChemistryJournal of Bacteriology
- 1 January 1979
A high activity of meso-alpha-epsilon-diaminopimelate dehydrogenase was found in extracts of Bacillus sphaericus, Brevibacterium sp., Corynebacterium glutamicum, and Proteus vulgaris among bacteria…
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