Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Kenichi Ishiwata"'
Autor:
Masanobu Arita, Mika Ihara, Aya Mizukuchi, Kenichi Ishiwata, Hiroko Kawana, Yukihiko Itoh, Misaki Ohnishi
Publikováno v:
Journal for the Integrated Study of Dietary Habits. 16:108-113
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::77a7a40c1f647cff96d35f6f53f8d31b
https://doi.org/10.2740/jisdh.16.108
https://doi.org/10.2740/jisdh.16.108
Publikováno v:
Journal of Fermentation and Bioengineering. 72:147-151
The tyrosine phenol-lyase (TPL) gene of Citrobacter freundii was cloned and the complete nucleotide sequence of the TPL gene was determined. The TPL gene consists of 1368bp (456 amino acids). The deduced amino acid sequence of TPL was compared with t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e9d7bd48fd1caf3b2df1ac6bea0a6c73
https://doi.org/10.1016/0922-338x(91)90207-w
https://doi.org/10.1016/0922-338x(91)90207-w
Publikováno v:
Biotechnology Letters. 12:185-190
The tryptophan synthase genes,trpA andtrpB, from a moderate thermophile,Bacillusstearothermophilus IFO13737, were expressed efficiently inEscherichiacoli. The recombinant tryptophan synthase amounted to 22% of the soluble cellular protein, and was pu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::40882d03fd4d161c928c764c049bdbfa
https://doi.org/10.1007/bf01026796
https://doi.org/10.1007/bf01026796
Publikováno v:
Agricultural and Biological Chemistry. 53:2941-2948
The tryptophan synthase genes, trpA and trpB, of Bacillus stearothermophilus IFO13737 were cloned by transformation of tryptophan auxotrophic mutations of the trp genes into Escherichia coli. The genes are located in the order of trpB and trp A, acco
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5c71ee3f2e6256a8835c70618d83db43
https://doi.org/10.1271/bbb1961.53.2941
https://doi.org/10.1271/bbb1961.53.2941
Publikováno v:
Agricultural and Biological Chemistry. 53:2941-2948
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a00300ffe52721e0104ff709bc826e5e
https://doi.org/10.1080/00021369.1989.10869796
https://doi.org/10.1080/00021369.1989.10869796
Publikováno v:
Journal of Fermentation and Bioengineering. 67:169-172
Tryptophan synthase of Escherichia coli catalyzes the synthesis of l -cysteine from various β-substituted- l -alanines (e.g., l -serine) and sulfides (e.g., sodium hydrosulfide). Not only l -serine but also O- methyl- l -serine , O- acetyl- l -serin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::85e36835d511a7209ef1e88145400402
https://doi.org/10.1016/0922-338x(89)90116-5
https://doi.org/10.1016/0922-338x(89)90116-5
Publikováno v:
Journal of Fermentation and Bioengineering. 68:84-87
Synthesis of S -carboxymethyl)- l -cysteine ( l -CMC) from L-serine with tryptophan synthase was studied. In the β-replacement reaction l -serine catalyzed by tryptophan synthase of Escherichia coli , thioglycolic acid was a poor substrate but alkyl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::60a0196c103021d95a9b720d06cf178f
https://doi.org/10.1016/0922-338x(89)90052-4
https://doi.org/10.1016/0922-338x(89)90052-4