A5014155960- Amino Acid Enzymes and Metabolism
- Microbial metabolism and enzyme function
- Enzyme Structure and Function
- Porphyrin Metabolism and Disorders
- Chemical Reactions and Isotopes
- Biochemical Acid Research Studies
- Polyamine Metabolism and Applications
- Biochemical and Molecular Research
- Enzyme Production and Characterization
- RNA Interference and Gene Delivery
- Peptidase Inhibition and Analysis
- Metabolism and Genetic Disorders
- Hemoglobin structure and function
- Advanced biosensing and bioanalysis techniques
- Tryptophan and brain disorders
- Protein Structure and Dynamics
- Metalloenzymes and iron-sulfur proteins
- Enzyme Catalysis and Immobilization
- Chemical Synthesis and Analysis
- Microbial Metabolic Engineering and Bioproduction
- Glycosylation and Glycoproteins Research
- Monoclonal and Polyclonal Antibodies Research
- Biopolymer Synthesis and Applications
- Metal-Catalyzed Oxygenation Mechanisms
- Axon Guidance and Neuronal Signaling
Osaka University
2014-2025
Osaka Research Institute of Industrial Science and Technology
2009-2023
Palacký University Olomouc
2014-2017
Ryukoku University
2017
John Wiley & Sons (United States)
2016
Bioengineering Center
2016
National Center for Genetic Engineering and Biotechnology
2016
Hudson Institute
2016
Centre of the Region Haná for Biotechnical and Agricultural Research
2015
Kyoto University
1988-2011
The crystal structures of the copper enzyme phenylethylamine oxidase from Gram-positive bacterium Arthrobacter globiformis (AGAO) have been determined and refined for three forms enzyme: holoenzyme in its active form (at 2.2 Å resolution), an inactive 2.8 apoenzyme resolution). has a topaquinone (TPQ) cofactor formed by post-translational modification tyrosine residue presence Cu2+. Significant differences between AGAO are limited to site. polypeptide fold is closely similar those amine...
The quinone of 2,4,5-trihydroxyphenylalanine (topa), recently identified as the covalently bound redox cofactor in copper amine oxidases, is encoded by a specific tyrosine codon. To elucidate mechanism its formation, recombinant phenylethylamine oxidase Arthrobacter globiformis has been overproduced Escherichia coli and purified Cu(2+)-deficient form. inactive precursor enzyme thus obtained was dramatically activated upon incubation with Cu2+, concomitantly formation topa at position...
Previously, we reported NELL-1 as a novel molecule overexpressed during premature cranial suture closure in patients with craniosynostosis (CS), one of the most common congenital craniofacial deformities. Here describe creation and analysis transgenic mice overexpressing Nell-1. Nell-1 animals exhibited CS-like phenotypes that ranged from simple to compound synostoses. Histologically, osteogenic fronts abnormally closing/closed sutures these revealed calvarial overgrowth overlap along...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTThermostable alanine racemase from Bacillus stearothermophilus: molecular cloning of the gene, enzyme purification, and characterizationKenji Inagaki, Katsuyuki Tanizawa, Bernard Badet, Christopher T. Walsh, Hidehiko Tanaka, Kenji SodaCite this: Biochemistry 1986, 25, 11, 3268–3274Publication Date (Print):June 3, 1986Publication History Published online1 May 2002Published inissue 3 June...
When establishing the most appropriate cells from huge numbers of a cell library for practical use in regenerative medicine and production various biopharmaceuticals, heterogeneity often found an isogenic population limits refinement clonal culture. Here, we demonstrated high-throughput screening suitable by automated undisruptive single-cell analysis isolation system, followed expansion isolated single cells. This system enabled establishment cells, such as embryonic stem with highest...
The crystal structure of the heterotrimeric quinohemoprotein amine dehydrogenase from Paracoccus denitrificans has been determined at 2.05-Å resolution. Within an 82-residue subunit is contained unusual redox cofactor, cysteine tryptophylquinone (CTQ), consisting orthoquinone-modified tryptophan side chain covalently linked to a nearby chain. surrounded on three sides by 489-residue, four-domain that includes diheme cytochrome c . Both subunits sit surface third subunit, 337-residue...
The role of the active site Cu(2+) phenylethylamine oxidase from Arthrobacter globiformis (AGAO) has been studied by substitution with other divalent cations, where we were able to remove >99.5% site. enzymes reconstituted Co(2+) and Ni(2+) (Co- Ni-AGAO) exhibited 2.2 0.9% activities, respectively, original Cu(2+)-enzyme (Cu-AGAO), but their K(m) values for amine substrate dioxygen comparable. X-ray crystal structures Co- Ni-AGAO solved at 2.0-1.8 A resolution. These revealed changes in...
D-Amino acid aminotransferase was found in several thermophilic Bacillus species and purified to homogeneity from the best producer, sp. YM-1, which newly isolated a sauna dust. The enzyme has molecular weight of about 62,000 consists two subunits identical (30,000). It catalyzes transamination between various D-amino acids alpha-keto acids, although substrate specificity is narrower than mesophile, sphaericus (Yonaha, K., Misono, H., Yamamoto, T., Soda, K. (1975) J. Biol. Chem. 250,...
By the yeast two-hybrid screening of a rat brain cDNA library with regulatory domain protein kinase C ζ (PKCζ) as bait, we have cloned gene coding for novel PKCζ-interacting homologous to Caenorhabditis elegans UNC-76 involved in axonal outgrowth and fasciculation. The designated FEZ1 (fasciculation elongation zeta-1) consisting 393 amino acid residues shows high Asp/Glu content contains several regions predicted form amphipathic helices. Northern blot analysis has revealed that mRNA is...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTAlanine dehydrogenases from two Bacillus species with distinct thermostabilities: molecular cloning, DNA and protein sequence determination, structural comparison other NAD(P)+-dependent dehydrogenasesShunichi Kuroda, Katsuyuki Tanizawa, Hidehiko Tanaka, Kenji Soda, Yonekazu SakamotoCite this: Biochemistry 1990, 29, 4, 1009–1015Publication Date (Print):January 30, 1990Publication History Published online1 May 2002Published inissue 30 January...
The crystal structure of a quinohemoprotein amine dehydrogenase from Pseudomonas putida has been determined at 1.9-A resolution. enzyme comprises three non-identical subunits: four-domain alpha-subunit that harbors di-heme cytochrome c, seven-bladed beta-propeller beta-subunit provides part the active site, and small gamma-subunit contains novel cross-linked, proteinous quinone cofactor, cysteine tryptophylquinone. More surprisingly, catalytic additional chemical cross-links encage...
The gene for thermostable D-amino acid aminotransferase from a thermophile, Bacillus species YM-1 was cloned and expressed efficiently in Escherichia coli. entire covalent structure of the enzyme determined nucleotide sequence mostly confirmed by amino sequences tryptic peptides product. polypeptide is composed 282 residues with calculated molecular weight 32,226. Comparison primary those various proteins registered protein data bank revealed significant homology between L-branched chain E....
NELL1 is an extracellular protein inducing osteogenic differentiation and bone formation of osteoblastic cells. To elucidate the intracellular signaling cascade evoked by NELL1, we have shown that transiently activates MAPK cascade, induces phosphorylation Runx2, promotes rapid accumulation Tyr-phosphorylated proteins. Unlike BMP2, does not activate Smad cascade. These findings suggest upon binding to a specific receptor transduces signal through activation certain Tyr-kinases associated...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTGene cloning and sequence determination of leucine dehydrogenase from Bacillus stearothermophilus structural comparison with other NAD(P)+-dependent dehydrogenasesShinji Nagata, Katsuyuki Tanizawa, Nobuyoshi Esaki, Yonekazu Sakamoto, Toshihisa Ohshima, Hidehiko Tanaka, Kenji SodaCite this: Biochemistry 1988, 27, 25, 9056–9062Publication Date (Print):December 13, 1988Publication History Published online1 May 2002Published inissue 13 December...
Although bacterial and mammalian glycogensynthases differ in the primary structure specificity for glucosyl donor, lysyl residues identified at their substrate-binding sites by affinity labeling are present a conserved tetrapeptide sequence, Lys-X-Gly-Gly, where X is residue not (Tagaya, M., Nakano, K.,