Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Hisaaki Mihara"'
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 84:2303-2310
Enzymes related to β-hydroxyacid dehydrogenases/3-hydroxyisobutyrate dehydrogenases are ubiquitous, but most of them have not been characterized. An uncharacterized protein with moderate sequence similarities to Gluconobacter oxydans succinic semial
Publikováno v:
Journal of Nutritional Science and Vitaminology. 61:506-510
Glycine oxidase, encoded by the thiO gene, participates in the biosynthesis of thiamin by providing glyoxyl imine to form the thiazole moiety of thiamin. We have purified and characterized ThiO from Pseudomonas putida KT2440. It has a monomeric struc
Publikováno v:
Selenium ISBN: 9783319412818
Selenocysteine lyase is a pyridoxal 5′-phosphate-dependent enzyme catalyzing the degradation of l-selenocysteine to l-alanine and elemental selenium. It is unique in that it acts exclusively on l-selenocysteine but not on its sulfur counterpart, l-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0294bb97cb35c4b4df68342587a022f2
https://doi.org/10.1007/978-3-319-41283-2_10
https://doi.org/10.1007/978-3-319-41283-2_10
Publikováno v:
Bioscience, biotechnology, and biochemistry. 80(3)
4-Methyl-5-hydroxyethylthiazole kinase (ThiM) participates in thiamin biosynthesis as the key enzyme in its salvage pathway. We purified and characterized ThiM from Escherichia coli. It has broad substrate specificity toward various nucleotides and s
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
Publikováno v:
Journal of Biochemistry. 148:371-379
Like an alpinist continuously seeking virgin peaks to climb, Kenji Soda has investigated a variety of unique enzymes for which there was little or no information available; and by doing so he opened up a variety of new fields in enzyme science and te
Publikováno v:
Tetrahedron: Asymmetry. 17:1775-1779
A new enzymatic system for the synthesis of enantiomerically pure cyclic amino acids (CAA) from the corresponding diamino acids or racemic CAA is described. α,ω-Diamino acids were oxidized to α-keto acids with amino acid oxidases (AAO). The α-ket
Autor:
Hiroshi Kawabata, Ryoma Miyake, Yasushi Tani, Makoto Ueda, Hisaaki Mihara, Koichiro Omatsu, Shigeki Saito
Publikováno v:
Journal of biochemistry. 157(4)
Fish have a complex self-defense mechanism against microbial invasion. Recently, l-lysine α-oxidases have been identified from a number of fish species as a novel type of antibacterial protein in the integument. These enzymes exhibit strict substrat
Publikováno v:
Journal of Molecular Catalysis B: Enzymatic. 23:367-372
Mouse selenocysteine lyase (SCL) catalyzes the decomposition of l -selenocysteine into l -alanine and selenium with pyridoxal 5′-phosphate as a coenzyme. When using SCL as bait in a yeast two-hybrid screening method, major urinary protein I (MUP-I)
Autor:
Hisaaki Mihara, Tatsuo Kurihara, Thressa C. Stadtman, Nobuyoshi Esaki, Umechiyo Tokumoto, Robert A. J. D. Kennedy, Gerard M. Lacourciere, Yasuhiro Takahashi, Shin-ichiro Kato
Publikováno v:
Proceedings of the National Academy of Sciences. 99:6679-6683
Three NifS-like proteins, IscS, CSD, and CsdB, from Escherichia coli catalyze the removal of sulfur and selenium from l -cysteine and l -selenocysteine, respectively, to form l -alanine. These enzymes are proposed to function as sulfur-delivery prote