Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Hisaaki Mihara"'
Autor:
Hisaaki Mihara, Ryuta Tobe
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1862:2433-2440
Background Selenophosphate, the key selenium donor for the synthesis of selenoprotein and selenium-modified tRNA, is produced by selenophosphate synthetase (SPS) from ATP, selenide, and H2O. Although free selenide can be used as the in vitro selenium
Publikováno v:
Applied Microbiology and Biotechnology. 91:47-61
Cysteine desulfurases are pyridoxal 5'-phosphate-dependent homodimeric enzymes that catalyze the conversion of L-cysteine to L-alanine and sulfane sulfur via the formation of a protein-bound cysteine persulfide intermediate on a conserved cysteine re
Autor:
Shin-ichiro Kato, Hiroshi Kanazawa, Hisaaki Mihara, Umechiyo Tokumoto, Shinobu Nomura, Hiroshi Matsubara, Tatsuo Kurihara, Nobuyoshi Esaki, Yoshiko Minami, Yasuhiro Takahashi
Publikováno v:
Journal of Biochemistry. 131:713-719
The assembly of iron-sulfur (Fe-S) clusters is mediated by complex machinery which, in Escherichia coli, is encoded by the iscRSUA-hscBA-fdx-ORF3 gene cluster. Here, we demonstrate the network of protein-protein interactions among the components invo
Autor:
Shin-ichiro Kato, Nobuyoshi Esaki, Tohru Yoshimura, Umechiyo Tokumoto, Yasuhiro Takahashi, Tatsuo Kurihara, Hisaaki Mihara
Publikováno v:
Proceedings of the National Academy of Sciences. 99:5948-5952
IscS and IscU from Escherichia coli cooperate with each other in the biosynthesis of iron-sulfur clusters. IscS catalyzes the desulfurization of l -cysteine to produce l -alanine and sulfur. Cys-328 of IscS attacks the sulfur atom of l -cysteine, and
Publikováno v:
Biochemistry. 39:1263-1273
Escherichia coli CsdB, a NifS homologue with a high specificity for L-selenocysteine, is a pyridoxal 5'-phosphate (PLP)-dependent dimeric enzyme that belongs to aminotransferases class V in fold-type I of PLP enzymes and catalyzes the decomposition o
Publikováno v:
Journal of Biological Chemistry. 274:14768-14772
Selenocysteine lyase is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes the exclusive decomposition of L-selenocysteine to L-alanine and elemental selenium. An open reading frame, named csdB, from Escherichia coli encodes a putative pr
Autor:
Toshiaki Tokimatsu, Susumu Goto, Hisaaki Mihara, Takeshiko Bayashi, Minoru Kanehisa, Masahiro Hattori, Masaaki Kotera
Publikováno v:
Scopus-Elsevier
Many cofactors and nucleotides containing sulfur atoms are known to have important functions in a variety of organisms. Recently, the biosynthetic pathways of these sulfur containing compounds have been revealed, where many enzymes relay sulfur atoms
Autor:
Hisaaki Mihara, Nobuyoshi Esaki, Tatsuo Kurihara, Wanjiao Zhang, Alexander Urban, Silke Leimkühler
The persulfide sulfur formed on an active site cysteine residue of pyridoxal 5'-phosphate-dependent cysteine desulfurases is subsequently incorporated into the biosynthetic pathways of a variety of sulfur-containing cofactors and thionucleosides. In
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63f7b559d365fee4a0b3347dff84fa8c
https://publishup.uni-potsdam.de/frontdoor/index/index/docId/31450
https://publishup.uni-potsdam.de/frontdoor/index/index/docId/31450
Publikováno v:
Biochemical and biophysical research communications. 372(3)
Inactivation of iscS encoding cysteine desulfurase results in a slow growth phenotype associated with the deficiency of iron–sulfur clusters, thiamine, NAD, and tRNA thionucleosides in Escherichia coli . However, the other roles of iscS in vivo are
Publikováno v:
Biochimica et biophysica acta. 1647(1-2)
Cysteine desulfurase plays a principal role in the assembly of iron–sulfur clusters by mobilizing the sulfur atom of l -cysteine. The active site cysteine residue of the enzyme attacks the sulfur atom of l -cysteine to form a cysteine persulfide re