Zobrazeno 1 - 10 of 43 pro vyhledávání: '"Yutaro Motokawa"'
1
Crystal Structure of Lipoate-Protein Ligase A from Escherichia coli
Autor: Atsushi Nakagawa, Yutaro Motokawa, Sachiko Toma, Kazuko Fujiwara, Kazuko Okamura-Ikeda, Hisaaki Taniguchi
Publikováno v: Journal of Biological Chemistry. 280:33645-33651
Lipoate-protein ligase A (LplA) catalyzes the formation of lipoyl-AMP from lipoate and ATP and then transfers the lipoyl moiety to a specific lysine residue on the acyltransferase subunit of α-ketoacid dehydrogenase complexes and on H-protein of the
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a9886629ca14b0f74ee922c6f2782e04
https://doi.org/10.1074/jbc.m505010200
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2
Crystal structure of lipoate-protein ligase A from Escherichia coli : Determination of the lipoic acid-binding site
Autor: Kazuko, Fujiwara, Sachiko, Toma, Kazuko, Okamura-Ikeda, Yutaro, Motokawa, Atsushi, Nakagawa, Hisaaki, Taniguchi
Publikováno v: Journal of Biological Chemistry. 280(39):33645-33651
This research was originally published in Journal of Biological Chemistry. Kazuko Fujiwara, Sachiko Toma, Kazuko Okamura-Ikeda, Yutaro Motokawa, Atsushi Nakagawa and Hisaaki Taniguchi. Crystal structure of lipoate-protein ligase A from Escherichia co
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::51a4d9f77ddc58f19ad8a4f87bd16a05
https://hdl.handle.net/11094/73652
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3
Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene
Autor: Mikio Suzuki, Tsutomu Fujiwara, Yutaro Motokawa, Kazuko Fujiwara, Kazuko Okamura-Ikeda, Ei-ichi Takahashi, Yasuyo Okumachi
Publikováno v: European Journal of Biochemistry. 260:761-767
Lipoyltransferase catalyzes the transfer of the lipoyl group from lipoyl-AMP to the lysine residue of the lipoate-dependent enzymes. We isolated human lipoyltransferase cDNA and genomic DNA. The cDNA insert contained a 1119-base pair open reading fra
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e6afaaf5a4490e9d67af4f9739bdc86
https://doi.org/10.1046/j.1432-1327.1999.00204.x
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4
Cloning and Expression of a cDNA Encoding Bovine Lipoyltransferase
Autor: Kazuko Okamura-Ikeda, Yutaro Motokawa, Kazuko Fujiwara
Publikováno v: Journal of Biological Chemistry. 272:31974-31978
Lipoyltransferase catalyzes the transfer of the lipoyl group from lipoyl-AMP to the specific lysine residue of the lipoate-dependent enzymes. We have isolated lipoyltransferase I (LipTI) and II (LipTII) from bovine liver (Fujiwara, K., Okamura-Ikeda,
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f8d75a5d5015d468338f9395f5fef6c
https://doi.org/10.1074/jbc.272.51.31974
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5
Molecular cloning of a cDNA encoding chicken T-protein of the glycine cleavage system and expression of the functional protein in Escherichia coli. Effect of mRNA secondary structure in the translational initiation region on expression
Autor: Kazuko Fujiwara, Kazuko Okamura-Ikeda, Yutaro Motokawa
Publikováno v: Journal of Biological Chemistry. 267:18284-18290
DNA clones encoding chicken T-protein of the glycine cleavage system were isolated from chicken liver lambda gt10 cDNA libraries. Three overlapping clones provided an open reading frame of 1176 nucleotides that predicts a polypeptide of 392 amino aci
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cfa88b767516bf68ba12e1bc23db7435
https://doi.org/10.1016/s0021-9258(19)36957-1
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6
Lipoylation of H-protein of the glycine cleavage system The effect of site-directed mutagenesis of amino acid residues around the lipoyllysine residue on the lipoate attachment
Autor: Yutaro Motokawa, Kazuko Fujiwara, Kazuko Okamura-Ikeda
Publikováno v: FEBS Letters. 293:115-118
H-protein of the glycine cleavage system has lipoic acid on the Lys59 residue. Comparison of amino acid sequences around the lipoate attachment site of H-proteins from various sources and acyltransferases of α-keto acid dehydrogenase complexes indic
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d73e8f7a9ed8bb7513d4bf40868ec0d
https://doi.org/10.1016/0014-5793(91)81164-4
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7
Glycine cleavage system: reaction mechanism, physiological significance, and hyperglycinemia
Autor: Yutaro Motokawa, Tadashi Yoshida, Goro Kikuchi, Koichi Hiraga
Publikováno v: Proceedings of the Japan Academy. Series B, Physical and Biological Sciences
The glycine cleavage system catalyzes the following reversible reaction: Glycine + H(4)folate + NAD(+) 5,10-methylene-H(4)folate + CO(2) + NH(3) + NADH + H(+)The glycine cleavage system is widely distributed in animals, plants and bacteria and consis
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d093fda417c233c7f06941e210af148
https://pubmed.ncbi.nlm.nih.gov/18941301
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10
Purification, characterization, and cDNA cloning of lipoate-activating enzyme from bovine liver
Autor: Kazuko Fujiwara, Kazuko Okamura-Ikeda, Yutaro Motokawa, Shinji Takeuchi
Publikováno v: The Journal of biological chemistry. 276(31)
In mammals, lipoate-activating enzyme (LAE) catalyzes the activation of lipoate to lipoyl-nucleoside monophosphate. The lipoyl moiety is then transferred to the specific lysine residue of lipoate-dependent enzymes by the action of lipoyltransferase.
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2e446fa959927eb134432a2d226f81d
https://pubmed.ncbi.nlm.nih.gov/11382754
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