Search Results - "Fukasawa, Kayoko M"

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  1. 1

    Flexibility of the coordination geometry around the cupric ions in Cu(II)-rat dipeptidyl peptidase III is important for the expression of enzyme activity by Hirose, Junzo, Hata, Toshiyuki, Kawaoka, Chie, Ikeura, Tomohiro, Kitahara, Suguru, Horii, Kozue, Tomida, Hisao, Iwamoto, Hiroyuki, Ono, Yukio, Fukasawa, Kayoko M.

    Published in Archives of biochemistry and biophysics (01-09-2012)
    “…► Dipeptidyl peptidase III has the unique metal-binding motif (HELLGH). ► The formations of the enzyme–metal–substrate complex. ► The flexibility of the…”
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  2. 2

    In rat dipeptidyl peptidase III, His⁵⁶⁸ is essential for catalysis, and Glu⁵⁰⁷ or Glu⁵¹² stabilizes the coordination bond between His⁴⁵⁵ or His⁴⁵⁰ and zinc ion by Fukasawa, Kayoko M, Hirose, Junzo, Hata, Toshiyuki, Ono, Yukio

    Published in Biochimica et biophysica acta (01-10-2010)
    “…Dipeptidyl peptidase (DPP) III is a zinc-dependent exopeptidase that has a unique motif, "HELLGH," as the zinc-binding site. In the present study, a…”
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  3. 3

    Aspartic Acid 405 Contributes to the Substrate Specificity of Aminopeptidase B by Fukasawa, Kayoko M, Hirose, Junzo, Hata, Toshiyuki, Ono, Yukio

    Published in Biochemistry (Easton) (26-09-2006)
    “…Aminopeptidase B (EC 3.4.11.6, ApB) specifically cleaves in vitro the N-terminal Arg or Lys residue from peptides and synthetic derivatives. Ap B was shown to…”
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  4. 4

    Characterization of the Metal-Binding Site in Aminopeptidase B by Hirose, Junzo, Ohsaki, Takamichi, Nishimoto, Naoyo, Matuoka, Shouji, Hiromoto, Takashi, Yoshida, Takahide, Minoura, Takatosi, Iwamoto, Hiroyuki, Fukasawa, Kayoko M.

    Published in Biological & Pharmaceutical Bulletin (01-12-2006)
    “…A recombinant rat aminopeptidase-B (Ap-B) was expressed as a glutathione S-transferase (GST) fusion protein in Escherichia coli BL21 harboring a plasmid…”
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  5. 5

    Metal Preferences of Zinc-Binding Motif on Metalloproteases by Fukasawa, Kayoko M., Hata, Toshiyuki, Ono, Yukio, Hirose, Junzo

    Published in Journal of amino acids (01-01-2011)
    “…Almost all naturally occurring metalloproteases are monozinc enzymes. The zinc in any number of zinc metalloproteases has been substituted by some other…”
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  6. 6

    Dipeptidyl peptidase III is a zinc metallo-exopeptidase. Molecular cloning and expression by Fukasawa, K, Fukasawa, K M, Kanai, M, Fujii, S, Hirose, J, Harada, M

    Published in Biochemical journal (15-01-1998)
    “…We have purified dipeptidyl peptidase III (EC 3.4.14.4) from human placenta. It had a pH optimum of 8.8 and readily hydrolysed Arg-Arg-beta-naphthylamide…”
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    Characterization of the Metal-Substituted Dipeptidyl Peptidase III (Rat Liver) by Hirose, Junzo, Iwamoto, Hiroyuki, Nagao, Ikuko, Enmyo, Kanako, Sugao, Hidenori, Kanemitu, Nobuharu, Ikeda, Keiichi, Takeda, Mitsunori, Inoue, Masaki, Ikeda, Tomoyuki, Matsuura, Fumito, Fukasawa, Kayoko M, Fukasawa, Katsuhiko

    Published in Biochemistry (Easton) (02-10-2001)
    “…Dipeptidyl peptidase III (DPP III) (EC 3.4.14.4), which has a HELLGH-E (residues 450−455, 508) motif as the zinc binding site, is classified as a zinc…”
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  9. 9

    Characterization of a functionally expressed dipeptidyl aminopeptidase III from Drosophila melanogaster by Mazzocco, Claire, Fukasawa, Kayoko M., Auguste, Patrick, Puiroux, Jacques

    Published in European journal of biochemistry (01-07-2003)
    “…A Drosophila melanogaster cDNA clone (GH01916) encoding a putative 723‐residue long (82 kDa) protein (CG 7415) and displaying 50% identity with mammalian…”
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  10. 10

    Identification and characterization of two dipeptidyl‐peptidase III isoforms in Drosophila melanogaster by Mazzocco, Claire, Gillibert‐Duplantier, Jennifer, Neaud, Veronique, Fukasawa, Kayoko M., Claverol, Stéphane, Bonneu, Marc, Puiroux, Jacques

    Published in The FEBS journal (01-03-2006)
    “…Dipeptidyl‐peptidase III (DPP III) hydrolyses small peptides with a broad substrate specificity. It is thought to be involved in a major degradation pathway of…”
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  11. 11

    The HELLGH Motif of Rat Liver Dipeptidyl Peptidase III Is Involved in Zinc Coordination and the Catalytic Activity of the Enzyme by Fukasawa, Katsuhiko, Fukasawa, Kayoko M, Iwamoto, Hiroyuki, Hirose, Junzo, Harada, Minoru

    Published in Biochemistry (Easton) (29-06-1999)
    “…The role of the HELLGH (residues 450−455) motif in the sequence of rat dipeptidyl peptidase III (EC 3.4.14.4) was investigated by replacing Glu451 with an…”
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  12. 12

    Molecular Cloning and Expression of Rat Liver Aminopeptidase B by Fukasawa, Kayoko M., Fukasawa, Katsuhiko, Kanai, Makoto, Fujii, Shingo, Harada, Minoru

    Published in The Journal of biological chemistry (29-11-1996)
    “…We isolated, by immunological screening of a Uni-ZAP XR cDNA library constructed from rat liver mRNAs, a cDNA clone with 2212 base pairs encoding…”
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  13. 13

    In rat dipeptidyl peptidase, His super(568) is essential for catalysis, and Glu super(507) or Glu super(512) stabilizes the coordination bond between His super(455) or His super(450) and zinc ion by Fukasawa, Kayoko M, Hirose, Junzo, Hata, Toshiyuki

    “…Dipeptidyl peptidase (DPP) III is a zinc-dependent exopeptidase that has a unique motif, "HELLGH," as the zinc-binding site. In the present study, a…”
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  14. 14

    Identification and quantification of alpha-amino adipic acid in bovine dentine phosphoprotein by Hiraoka, B Y, Fukasawa, K, Fukasawa, K M, Harada, M

    Published in Journal of biochemistry (Tokyo) (1980)
    “…A unique phosphoprotein, which contains an uncommon amino acid, alpha-amino adipic acid (alpha-AAA), was isolated from unerupted bovine teeth by extensive EDTA…”
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  15. 15

    In rat dipeptidyl peptidase III, His 568 is essential for catalysis, and Glu 507 or Glu 512 stabilizes the coordination bond between His 455 or His 450 and zinc ion by Fukasawa, Kayoko M., Hirose, Junzo, Hata, Toshiyuki, Ono, Yukio

    “…Dipeptidyl peptidase (DPP) III is a zinc-dependent exopeptidase that has a unique motif, “HELLGH,” as the zinc-binding site. In the present study, a…”
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  16. 16

    Identification of amino acid residues on Aminopeptidase B involved in binding to the substrate by Fukasawa, Kayoko M, Hirose, Junzo, Hata, Toshiyuki, Ono, Yukio

    Published in The FASEB journal (01-04-2007)
    “…Aminopeptidase B (EC 3.4.11.6, ApB) specifically cleaves in vitro the N‐terminal Arg or Lys residue from peptides and synthetic derivatives. Ap B has been…”
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  17. 17

    Complete nucleotide sequence of the mouse lactate dehydrogenase-A functional gene: comparison of the exon-intron organization of dehydrogenase genes by Fukasawa, Kayoko M, Li, Steven S.-L

    Published in Genetics (Austin) (01-05-1987)
    “…The complete sequence of 12,851 nucleotides of the mouse lactate dehydrogenase-A (LDH-A) gene has been determined. It includes eight exons, seven introns,…”
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  18. 18

    Molecular Nature of Spontaneous Mutations in Mouse Lactate Dehydrogenase-A Processed Pseudogenes by Fukasawa, Kayoko M, Tanimura, Masako, Sakai, Ikuya, Sharief, Farida S, Chung, Fu-Zon, Li, Steven S.-L

    Published in Genetics (Austin) (01-01-1987)
    “…The presence of at least ten mouse LDH-A pseudogenes was demonstrated in the genomic blot analysis, and four different processed pseudogenes have thus far been…”
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    Comparison of dipeptidyl peptidase IV prepared from pig liver and kidney by Fukasawa, K M, Fukasawa, K, Hiraoka, B Y, Harada, M

    Published in Biochimica et biophysica acta (01-01-1981)
    “…Dipeptidyl peptidase IV (dipeptidylpeptide hydrolase, EC 3.4.14.-) has been purified from the microsomal fraction of pig liver, using an immunoaffinity…”
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