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- Publications
- Influence
Gene cloning, biochemical characterization and physiological role of a thermostable low-specificity L-threonine aldolase from Escherichia coli.
- J. Liu, T. Dairi, N. Itoh, M. Kataoka, S. Shimizu, H. Yamada
- Biology, Medicine
- European journal of biochemistry
- 1 July 1998
The ltaE gene encoding for a thermostable low-specificity L-threonine aldolase, which catalyzes the cleavage of L-threonine/L-allo-threonine to glycine and acetaldehyde, was cloned from Escherichia… Expand
The prevalence of types I and II feline coronavirus infections in cats.
- T. Hohdatsu, S. Okada, Y. Ishizuka, H. Yamada, H. Koyama
- Biology, Medicine
- The Journal of veterinary medical science
- 15 June 1992
The types of feline coronaviruses that are prevalent throughout Japan were determined by competitive enzyme-linked immunosorbent assay (ELISA) using a monoclonal antibody (MAb) to feline infectious… Expand
Enzymatic synthesis of acrylamide: a success story not yet over.
- M. Kobayashi, T. Nagasawa, H. Yamada
- Chemistry, Medicine
- Trends in biotechnology
- 1992
The application of enzymatic transformations is attracting increasing attention. Until recently, such an approach has generally been confined to producing fine chemicals difficult to obtain through… Expand
Characterization of a new cobalt-containing nitrile hydratase purified from urea-induced cells of Rhodococcus rhodochrous J1.
- T. Nagasawa, K. Takeuchi, H. Yamada
- Chemistry, Medicine
- European journal of biochemistry
- 1 March 1991
A new cobalt-containing nitrile hydratase was purified from extracts of urea-induced cells from Rhodococcus rhodochrous J1 in seven steps. At the last step, the enzyme was crystallized by adding… Expand
Nitrile hydratase of Brevibacterium R312--purification and characterization.
- T. Nagasawa, K. Ryuno, H. Yamada
- Chemistry, Medicine
- Biochemical and biophysical research…
- 30 September 1986
Nitrile hydratase was purified and crystallized from the crude extract of Brevibacterium R312 and found to be homogeneous by the results of disc gel electrophoresis, analytical ultracentrifuge and… Expand
Primary structure of an aliphatic nitrile-degrading enzyme, aliphatic nitrilase, from Rhodococcus rhodochrous K22 and expression of its gene and identification of its active site residue.
- M. Kobayashi, N. Yanaka, T. Nagasawa, H. Yamada
- Biology, Medicine
- Biochemistry
- 22 September 1992
Peptides obtained by cleavage of a Rhodococcus rhodochrous K22 nitrilase, which acts on aliphatic nitriles such as acrylonitrile, crotonitrile, and glutaronitrile, have been sequenced. The data… Expand
Tyrosine phenol lyase. I. Purification, crystallization, and properties.
- H. Kumagai, H. Yamada, H. Matsui, H. Ohkishi, K. Ogata
- Chemistry, Medicine
- The Journal of biological chemistry
- 10 April 1970
Abstract Crystalline l-tyrosine phenol lyase (deaminating) was prepared from the cell extract of Escherichia intermedia A-21 grown in a medium supplemented with l-tyrosine. The purification procedure… Expand
Nitrilase from Rhodococcus rhodochrous J1. Sequencing and overexpression of the gene and identification of an essential cysteine residue.
- M. Kobayashi, H. Komeda, N. Yanaka, T. Nagasawa, H. Yamada
- Biology, Medicine
- The Journal of biological chemistry
- 15 October 1992
The amino acid sequences of the NH2 terminus and internal peptide fragments of a Rhodococcus rhodochrous J1 nitrilase were determined to prepare synthetic oligonucleotides as primers for the… Expand
Thermostable N-carbamoyl-D-amino acid amidohydrolase: screening, purification and characterization.
- J. Ogawa, M. Chung, S. Hida, H. Yamada, S. Shimizu
- Chemistry, Medicine
- Journal of biotechnology
- 30 November 1994
A thermostable N-carbamoyl-D-amino acid amidohydrolase was found in the cells of newly isolated bacterium. Blastobacter sp. A17p-4. The bacterium also showed D-specific hydantoinase activity. The… Expand
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, Medicine
- European journal of biochemistry
- 1 April 1997
The GLY1 gene of Saccharomyces cerevisiae is required for the biosynthesis of glycine for cell growth [McNeil, J. B., McIntosh, E. V., Taylor, B. V., Zhang, F-R., Tang, S. & Bognar, A. L. (1994) J.… Expand