Matsuzawa H - Search Results

1

Methionyl-tRNA synthetase gene from an extreme thermophile, Thermus thermophilus HB8. Molecular cloning, primary-structure analysis, expression in Escherichia coli, and site-directed mutagenesis.

Nureki O, Muramatsu T, Suzuki K, Kohda D, Matsuzawa H, Ohta T, Miyazawa T, Yokoyama S. Nureki O, et al. Among authors: matsuzawa h. J Biol Chem. 1991 Feb 15;266(5):3268-77. J Biol Chem. 1991. PMID: 1993699 Free article.

2

Molecular cloning and nucleotide sequence of the aminopeptidase T gene of Thermus aquaticus YT-1 and its high-level expression in Escherichia coli.

Motoshima H, Azuma N, Kaminogawa S, Ono M, Minagawa E, Matsuzawa H, Ohta T, Yamauchi K. Motoshima H, et al. Among authors: matsuzawa h. Agric Biol Chem. 1990 Sep;54(9):2385-92. Agric Biol Chem. 1990. PMID: 1368580 Free article.

3

Involvement of NH2-terminal pro-sequence in the production of active aqualysin I (a thermophilic serine protease) in Escherichia coli.

Lee YC, Miyata Y, Terada I, Ohta T, Matsuzawa H. Lee YC, et al. Among authors: matsuzawa h. Agric Biol Chem. 1991 Dec;55(12):3027-32. Agric Biol Chem. 1991. PMID: 1368764 Free article.

4

Glutamyl-tRNA synthetase from Thermus thermophilus HB8. Molecular cloning of the gltX gene and crystallization of the overproduced protein.

Nureki O, Suzuki K, Hara-Yokoyama M, Kohno T, Matsuzawa H, Ohta T, Shimizu T, Morikawa K, Miyazawa T, Yokoyama S. Nureki O, et al. Among authors: matsuzawa h. Eur J Biochem. 1992 Mar 1;204(2):465-72. doi: 10.1111/j.1432-1033.1992.tb16656.x. Eur J Biochem. 1992. PMID: 1541262 Free article.

5

Site-directed mutants, at position 166, of RTEM-1 beta-lactamase that form a stable acyl-enzyme intermediate with penicillin.

Adachi H, Ohta T, Matsuzawa H. Adachi H, et al. Among authors: matsuzawa h. J Biol Chem. 1991 Feb 15;266(5):3186-91. J Biol Chem. 1991. PMID: 1993691 Free article.

6

Unique precursor structure of an extracellular protease, aqualysin I, with NH2- and COOH-terminal pro-sequences and its processing in Escherichia coli.

Terada I, Kwon ST, Miyata Y, Matsuzawa H, Ohta T. Terada I, et al. Among authors: matsuzawa h. J Biol Chem. 1990 Apr 25;265(12):6576-81. J Biol Chem. 1990. PMID: 2182621 Free article.

7

Conformation of NAD+ bound to allosteric L-lactate dehydrogenase activated by chemical modification.

Koide S, Yokoyama S, Matsuzawa H, Miyazawa T, Ohta T. Koide S, et al. Among authors: matsuzawa h. J Biol Chem. 1989 May 25;264(15):8676-9. J Biol Chem. 1989. PMID: 2722793 Free article.

8

Determination of the positions of the disulfide bonds in aqualysin I (a thermophilic alkaline serine protease) of Thermus aquaticus YT-1.

Kwon ST, Matsuzawa H, Ohta T. Kwon ST, et al. Among authors: matsuzawa h. J Biochem. 1988 Oct;104(4):557-9. doi: 10.1093/oxfordjournals.jbchem.a122509. J Biochem. 1988. PMID: 3240997 Free article.

9

Nucleotide sequence of the gene for aqualysin I (a thermophilic alkaline serine protease) of Thermus aquaticus YT-1 and characteristics of the deduced primary structure of the enzyme.

Kwon ST, Terada I, Matsuzawa H, Ohta T. Kwon ST, et al. Among authors: matsuzawa h. Eur J Biochem. 1988 May 2;173(3):491-7. doi: 10.1111/j.1432-1033.1988.tb14025.x. Eur J Biochem. 1988. PMID: 3286255 Free article.

Aqualysin I is an alkaline serine protease which is secreted into the culture medium by Thermus aquaticus YT-1, an extreme thermophile [Matsuzawa, H., Hamaoki, M. & Ohta, T. (1983) Agric. Biol. Chem. 47, 25-28]. The gene encoding aqualysin I was cloned into Esch …

Aqualysin I is an alkaline serine protease which is secreted into the culture medium by Thermus aquaticus YT-1, an extreme thermophile [M …

10

Involvement of the conserved histidine-188 residue in the L-lactate dehydrogenase from Thermus caldophilus GK24 in allosteric regulation by fructose 1,6-bisphosphate.

Schroeder G, Matsuzawa H, Ohta T. Schroeder G, et al. Among authors: matsuzawa h. Biochem Biophys Res Commun. 1988 May 16;152(3):1236-41. doi: 10.1016/s0006-291x(88)80417-0. Biochem Biophys Res Commun. 1988. PMID: 3377774

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