Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Masahiko, Goda"'
Autor:
Michihiko Kobayashi, Yoshiteru Hashimoto, Hideaki Hosaka, Hiroki Higashibata, Ken-Ichi Oinuma, Masahiko Goda
Publikováno v:
Journal of Biological Chemistry. 280:8660-8667
Two open reading frames (nhpS and acsA) were identified immediately downstream of the previously described Pseudomonas chlororaphis B23 nitrile hydratase (NHase) gene cluster (encoding aldoxime dehydratase, amidase, the two NHase subunits, and an unc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3810e53347785316a97f0d54f0377af8
https://doi.org/10.1074/jbc.m405686200
https://doi.org/10.1074/jbc.m405686200
Autor:
Kazunobu Konishi, Takumi Noguchi, Michihiko Kobayashi, Masahiko Goda, Yoshiteru Hashimoto, Hiroki Higashibata, Ken-Ichi Oinuma
Publikováno v:
Journal of Biological Chemistry. 278:29600-29608
Analysis of the nitrile hydratase gene cluster involved in nitrile metabolism of Pseudomonas chlororaphis B23 revealed that it contains one open reading frame encoding aldoxime dehydratase upstream of the amidase gene. The amino acid sequence deduced
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6fb448d29418e927b86a31b2b331fec8
https://doi.org/10.1074/jbc.m211832200
https://doi.org/10.1074/jbc.m211832200
Autor:
Yasuhito Iwahara, Sachio Herai, Masanori Takase, Michihiko Kobayashi, Masahiko Goda, Hiroki Higashibata, Yoshiteru Hashimoto
Publikováno v:
Journal of Biological Chemistry. 277:45860-45865
Isonitrile hydratase is a novel enzyme in Pseudomonas putida N19-2 that catalyzes the conversion of isonitriles to N-substituted formamides. Based on N-terminal and internal amino acid sequences, a 535-bp DNA fragment corresponding to a portion of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3a8be3d3b56df62447ebb4a3d213961c
https://doi.org/10.1074/jbc.m208571200
https://doi.org/10.1074/jbc.m208571200
Publikováno v:
Biochemical and Biophysical Research Communications. 253:662-666
While amides were reported to be completely inert as substrates for all nitrilases reported to date, the nitrilase from Rhodococcus rhodochrous J1, which catalyzes the hydrolytic cleavage of the C-N triple bond in nitrile to form acid and ammonium, w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce406a286072bef6674ac00d8d10c277
https://doi.org/10.1006/bbrc.1998.9834
https://doi.org/10.1006/bbrc.1998.9834
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 69:228-230
We investigated the optimum culture conditions for the production of a novel enzyme, N-substituted formamide deformylase, which acts mainly on N-benzylformamide, in Arthrobacter pascens F164. The highest enzyme activity was obtained when this strain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eda11329e806b559220c388f802c86a5
https://doi.org/10.1271/bbb.69.228
https://doi.org/10.1271/bbb.69.228
Autor:
Yoshiteru, Hashimoto, Hideaki, Hosaka, Ken-Ichi, Oinuma, Masahiko, Goda, Hiroki, Higashibata, Michihiko, Kobayashi
Publikováno v:
The Journal of biological chemistry. 280(10)
Two open reading frames (nhpS and acsA) were identified immediately downstream of the previously described Pseudomonas chlororaphis B23 nitrile hydratase (NHase) gene cluster (encoding aldoxime dehydratase, amidase, the two NHase subunits, and an unc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::805829f82a121f19c4ae6381a5ab87c6
https://pubmed.ncbi.nlm.nih.gov/15632196
https://pubmed.ncbi.nlm.nih.gov/15632196
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 101(38)
N-substituted formamide was produced through the hydration of an isonitrile by isonitrile hydratase in the isonitrile metabolism. The former compound was further degraded by a microorganism, strain F164, which was isolated from soil through an acclim
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a7dc87124925e201b915bbf5407cc31
https://pubmed.ncbi.nlm.nih.gov/15358859
https://pubmed.ncbi.nlm.nih.gov/15358859
Autor:
Ken-Ichi, Oinuma, Yoshiteru, Hashimoto, Kazunobu, Konishi, Masahiko, Goda, Takumi, Noguchi, Hiroki, Higashibata, Michihiko, Kobayashi
Publikováno v:
The Journal of biological chemistry. 278(32)
Analysis of the nitrile hydratase gene cluster involved in nitrile metabolism of Pseudomonas chlororaphis B23 revealed that it contains one open reading frame encoding aldoxime dehydratase upstream of the amidase gene. The amino acid sequence deduced
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::af259d2a530959a4e45cf824000ba20e
https://pubmed.ncbi.nlm.nih.gov/12773527
https://pubmed.ncbi.nlm.nih.gov/12773527
Autor:
Masahiko, Goda, Yoshiteru, Hashimoto, Masanori, Takase, Sachio, Herai, Yasuhito, Iwahara, Hiroki, Higashibata, Michihiko, Kobayashi
Publikováno v:
The Journal of biological chemistry. 277(48)
Isonitrile hydratase is a novel enzyme in Pseudomonas putida N19-2 that catalyzes the conversion of isonitriles to N-substituted formamides. Based on N-terminal and internal amino acid sequences, a 535-bp DNA fragment corresponding to a portion of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::cb24559b333a1dde6cb1c570531ee5e3
https://pubmed.ncbi.nlm.nih.gov/12244065
https://pubmed.ncbi.nlm.nih.gov/12244065
Publikováno v:
The Journal of biological chemistry. 276(26)
Isonitrile containing an N triple bond C triple bond was degraded by microorganism sp. N19-2, which was isolated from soil through a 2-month acclimatization culture in the presence of this compound. The isonitrile-degrading microorganism was identifi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::413463f854650bb44b90bd57b6602fb1
https://pubmed.ncbi.nlm.nih.gov/11306561
https://pubmed.ncbi.nlm.nih.gov/11306561