Search Results - "Gomi, Tomoharu"
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Modulation of H+,K+-ATPase activity by the molecular chaperone ERp57 highly expressed in gastric parietal cells
Published in FEBS letters (11-12-2013)“…•ERp57 is abundantly expressed in the apical membrane of gastric parietal cells.•ERp57 positively regulates H+,K+-ATPase activity apart from its chaperoning…”
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2
Catalytic Mechanism of Glycine N-Methyltransferase
Published in Biochemistry (Easton) (22-07-2003)“…Methyltransfer reactions are some of the most important reactions in biological systems. Glycine N-methyltransferase (GNMT) catalyzes the…”
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3
Deletion and Purification Studies to Elucidate the Structure of the Actinobacillus actinomycetemcomitans Cytolethal Distending Toxin
Published in Journal of biochemistry (Tokyo) (01-09-2004)“…Cytolethal distending toxin (CDT) is one of the exotoxins produced by Actinobacillus actinomycetemcomitans, an agent of localized aggressive periodontitis. We…”
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4
Cloning, bacterial expression, and unique structure of adenosylhomocysteine hydrolase-like protein 1, or inositol 1,4,5-triphosphate receptor-binding protein from mouse kidney
Published in Biochimica et biophysica acta (01-11-2008)“…Adenosylhomocysteine hydrolase (SAHase)-like protein 1 (SAH-L), also called inositol 1,4,5-triphosphate receptor-binding protein (IRBIT) is a novel protein…”
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5
Enzymatic Properties of Dipeptidyl Aminopeptidase IV Produced by the Periodontal Pathogen Porphyromonas gingivalis and Its Participation in Virulence
Published in Infection and Immunity (01-02-2000)“…Classifications Services IAI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit…”
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6
Crystal Structure of Guanidinoacetate Methyltransferase from Rat Liver: A Model Structure of Protein Arginine Methyltransferase
Published in Journal of molecular biology (05-07-2002)“…Guanidinoacetate methyltransferase (GAMT) is the enzyme that catalyzes the last step of creatine biosynthesis. The enzyme is found in abundance in the livers…”
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7
Solution structure of epiregulin and the effect of its C-terminal domain for receptor binding affinity
Published in FEBS letters (23-10-2003)“…Epiregulin (EPR), a novel member of epidermal growth factor (EGF) family, is a ligand for ErbB-1 and ErbB-4 receptors. The binding affinity of EPR for the…”
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Enzymatic and biochemical properties of a novel human serine dehydratase isoform
Published in Biochimica et biophysica acta (01-05-2006)“…A cDNA clone similar to human serine dehydratase (SDH) is deposited in the GenBank/EMBL databases, but its structural and functional bases remain unknown…”
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Reconstitution and Purification of Cytolethal Distending Toxin of Actinobacillus actinomycetemcomitans
Published in Microbiology and immunology (01-01-2001)“…Cytolethal distending toxin (CDT) has been found in various pathogenic bacterial species and causes a cell distending and a G2 arrest against eukaryotic cells…”
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10
Some biochemical and histochemical properties of human liver serine dehydratase
Published in The international journal of biochemistry & cell biology (01-03-2005)“…In rat, serine dehydratase (SDH) is abundant in the liver and known to be a gluconeogenic enzyme, while there is little information about the biochemical…”
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11
Catalytic Mechanism ofS-Adenosylhomocysteine Hydrolase
Published in The Journal of biological chemistry (21-06-2002)“…S-Adenosylhomocysteine hydrolase (AdoHcyase) catalyzes the hydrolysis ofS-adenosylhomocysteine to form adenosine and homocysteine. On the bases of crystal…”
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12
Inhibition of S-Adenosylhomocysteine Hydrolase by Acyclic Sugar Adenosine Analogue d-Eritadenine
Published in The Journal of biological chemistry (01-03-2002)“…d-Eritadenine (DEA) is a potent inhibitor (IC50 = 7 nm) ofS-adenosyl-l-homocysteine hydrolase (AdoHcyase). Unlike cyclic sugar Ado analogue inhibitors,…”
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Effects of Site-directed Mutagenesis on Structure and Function of Recombinant Rat Liver S-Adenosylhomocysteine Hydrolase
Published in The Journal of biological chemistry (13-10-2000)“…A site-directed mutagenesis, D244E, ofS-adenosylhomocysteine hydrolase (AdoHcyase) changes drastically the nature of the protein, especially the NAD+binding…”
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14
Identification of a lysine residue in the NADH-binding site of salicylate hydroxylase from Pseudomonas putida S-1
Published in Journal of biochemistry (Tokyo) (01-03-1995)“…Salicylate hydroxylase from Pseudomonas putida S-1 was irreversibly inactivated by trinitrobenzenesulfonic acid (TNBS). The reaction was linearly dependent on…”
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Catalytic mechanism of S-adenosylhomocysteine hydrolase: Roles of His 54, Asp130, Glu155, Lys185, and Aspl89
Published in The international journal of biochemistry & cell biology (01-11-2005)“…S-Adenosylhomocysteine hydrolase (AdoHcyase) catalyzes the hydrolysis of S-adenosylhomocysteine (AdoHcy) to form adenosine and homocysteine. The crystal…”
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16
Hydroxylation of o-halogenophenol and o-nitrophenol by salicylate hydroxylase
Published in Journal of biochemistry (Tokyo) (01-02-1991)“…Salicylate hydroxylase [EC 1.14.13.1] from Pseudomonas putida catalyzed the formation of catechol from substrate analogues such as o-nitro-, o-amino-, o-iodo-,…”
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Intermediate and mechanism of hydroxylation of o-iodophenol by salicylate hydroxylase
Published in Journal of biochemistry (Tokyo) (1991)“…Salicylate hydroxylase [EC 1.14.13.1] from Pseudomonas putida catalyzes the hydroxylation of salicylate, and also o-aminophenol, o-nitrophenol, and…”
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18
Serine hydroxymethyltransferase and threonine aldolase: are they identical?
Published in International Journal of Biochemistry and Cell Biology (01-03-2000)“…Serine hydroxymethyltransferase, a pyridoxal phosphate-dependent enzyme, catalyses the interconversion of serine and glycine, both of which are major sources…”
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Crystal Structure of S-Adenosylhomocysteine Hydrolase from Rat Liver
Published in Biochemistry (Easton) (29-06-1999)“…The crystal structure of rat liver S-adenosyl-l-homocysteine hydrolase (AdoHcyase, EC 3.3.1.1) which catalyzes the reversible hydrolysis of…”
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20
Catalytic Mechanism of Guanidinoacetate Methyltransferase: Crystal Structures of Guanidinoacetate Methyltransferase Ternary Complexes
Published in Biochemistry (Easton) (16-11-2004)“…Guanidinoacetate methyltransferase (GAMT) is the enzyme that catalyzes the last step of creatine biosynthesis. The enzyme is found in abundance in the livers…”
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