Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Ryuhei Nagata"'
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-8 (2018)
While most kinases are ATP-dependent some utilize pyrophosphate (PPi) instead. Here the authors structurally characterize a PPi-dependent kinase, identify its key recognition residues and find further PPi-dependent ribokinase family members with this
Externí odkaz:
https://doaj.org/article/679a3de9b2dc42ffa99617e22a2f9161
Publikováno v:
Biochemistry.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2d0287bf68893efeff05519a99e70c2f
https://doi.org/10.1021/acs.biochem.3c00025
https://doi.org/10.1021/acs.biochem.3c00025
Autor:
Ryuhei Nagata, Hironori Suemune, Masaya Kobayashi, Tetsuro Shinada, Kazuo Shin‐ya, Makoto Nishiyama, Tomoya Hino, Yusuke Sato, Tomohisa Kuzuyama, Shingo Nagano
Publikováno v:
Angewandte Chemie (International ed. in English). 61(20)
Some enzymes annotated as squalene synthase catalyze the prenylation of carbazole-3,4-quinone-containing substrates in bacterial secondary metabolism. Their reaction mechanisms remain unclear because of their low sequence similarity to well-character
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e096aee5372741fb871656577122c9e9
https://pubmed.ncbi.nlm.nih.gov/35235232
https://pubmed.ncbi.nlm.nih.gov/35235232
Autor:
Masahiro Fujihashi, Haruyuki Atomi, Ryuhei Nagata, Yasunobu Mori, Hiroki Kawamura, Takaaki Sato, Kunio Miki, Takayuki Fujita
Publikováno v:
J Bacteriol
Serine kinase catalyzes the phosphorylation of free serine (Ser) to produce O -phosphoserine (Sep). An ADP-dependent Ser kinase in the hyperthermophilic archaeon Thermococcus kodakarensis ( Tk -SerK) is involved in cysteine (Cys) biosynthesis and mos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::706fc5717f6229d9f4aea7a6ff8e2d1f
https://europepmc.org/articles/PMC8297531/
https://europepmc.org/articles/PMC8297531/
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-8 (2018)
Nature Communications
Nature Communications
Almost all kinases utilize ATP as their phosphate donor, while a few kinases utilize pyrophosphate (PPi) instead. PPi-dependent kinases are often homologous to their ATP-dependent counterparts, but determinants of their different donor specificities
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::776f1faad700167961f3f79f9a3d4814
https://doi.org/10.1038/s41467-018-04201-z
https://doi.org/10.1038/s41467-018-04201-z
Structural Study on the Reaction Mechanism of a Free Serine Kinase Involved in Cysteine Biosynthesis
Autor:
Haruyuki Atomi, Takaaki Sato, Hiroki Kawamura, Masahiro Fujihashi, Kunio Miki, Ryuhei Nagata, Takayuki Fujita
Publikováno v:
ACS chemical biology. 12(6)
A free serine kinase (SerK) is involved in l-cysteine biosynthesis in the hyperthermophilic archaeon Thermococcus kodakarensis. The enzyme converts ADP and l-serine (Ser) into AMP and O-phospho-l-serine (Sep), which is a precursor of l-cysteine. SerK
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29d6ca6433f9a804e7565b79c0c3babd
https://pubmed.ncbi.nlm.nih.gov/28358477
https://pubmed.ncbi.nlm.nih.gov/28358477
Autor:
Ryuhei NAGATA, Masahiro FUJIHASHI
Publikováno v:
KAGAKU TO SEIBUTSU. 56:779-780
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c29ee0188ee7303507efa0f97f77d96e
https://doi.org/10.1271/kagakutoseibutsu.56.779
https://doi.org/10.1271/kagakutoseibutsu.56.779
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 74:a196-a196
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::29a5625cdcd38e9c2a3521b8fdd226da
https://doi.org/10.1107/s0108767318098033
https://doi.org/10.1107/s0108767318098033
Publikováno v:
Biochemistry. 54(22)
The TK2285 protein from Thermococcus kodakarensis was recently characterized as an enzyme catalyzing the phosphorylation of myo-inositol. Only two myo-inositol kinases have been identified so far, the TK2285 protein and Lpa3 from Zea mays, both of wh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::11fcb62d56bc857173821cf645d9a186
https://pubmed.ncbi.nlm.nih.gov/25972008
https://pubmed.ncbi.nlm.nih.gov/25972008
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 70:C471-C471
The TK2285 protein from a hyperthermopilic archaeon Thermococcus kodakarensis is a myo-inositol kinase. Only two myo-inositol kinases have been identified so far. One is the TK2285 protein and the other is an enzyme from Zea mays. Both of them synthe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b3b23c27a4a568bb65345f5cf5b6e60d
https://doi.org/10.1107/s205327331409528x
https://doi.org/10.1107/s205327331409528x