Taguchi H - Search Results

1

Crystal structure of non-allosteric L-lactate dehydrogenase from Lactobacillus pentosus at 2.3 A resolution: specific interactions at subunit interfaces.

Uchikoba H, Fushinobu S, Wakagi T, Konno M, Taguchi H, Matsuzawa H. Uchikoba H, et al. Among authors: taguchi h. Proteins. 2002 Feb 1;46(2):206-14. doi: 10.1002/prot.1165. Proteins. 2002. PMID: 11807949

2

Purification and characterization of a thermostable carboxypeptidase (carboxypeptidase Taq) from Thermus aquaticus YT-1.

Lee SH, Minagawa E, Taguchi H, Matsuzawa H, Ohta T, Kaminogawa S, Yamauchi K. Lee SH, et al. Among authors: taguchi h. Biosci Biotechnol Biochem. 1992 Nov;56(11):1839-44. doi: 10.1271/bbb.56.1839. Biosci Biotechnol Biochem. 1992. PMID: 1369078 Free article.

3

Unusual amino acid substitution in the anion-binding site of Lactobacillus plantarum non-allosteric L-lactate dehydrogenase.

Taguchi H, Ohta T. Taguchi H, et al. Eur J Biochem. 1992 Nov 1;209(3):993-8. doi: 10.1111/j.1432-1033.1992.tb17373.x. Eur J Biochem. 1992. PMID: 1425707 Free article.

4

D-lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid dehydrogenase family. Cloning, sequencing, and expression in Escherichia coli of the D-lactate dehydrogenase gene of Lactobacillus plantarum.

Taguchi H, Ohta T. Taguchi H, et al. J Biol Chem. 1991 Jul 5;266(19):12588-94. J Biol Chem. 1991. PMID: 1840590 Free article.

5

Purification and characterization of aqualysin I (a thermophilic alkaline serine protease) produced by Thermus aquaticus YT-1.

Matsuzawa H, Tokugawa K, Hamaoki M, Mizoguchi M, Taguchi H, Terada I, Kwon ST, Ohta T. Matsuzawa H, et al. Among authors: taguchi h. Eur J Biochem. 1988 Feb 1;171(3):441-7. doi: 10.1111/j.1432-1033.1988.tb13809.x. Eur J Biochem. 1988. PMID: 3162211 Free article.

6

L-Lactate dehydrogenase from Thermus caldophilus GK24, an extremely thermophilic bacterium. Desensitization to fructose 1,6-bisphosphate in the activated state by arginine-specific chemical modification and the N-terminal amino acid sequence.

Taguchi H, Matsuzawa H, Ohta T. Taguchi H, et al. Eur J Biochem. 1984 Dec 3;145(2):283-90. doi: 10.1111/j.1432-1033.1984.tb08550.x. Eur J Biochem. 1984. PMID: 6499843 Free article.

Heat-stable and fructose-1,6-bisphosphate-activated L-lactate dehydrogenase (EC 1.1.1.27) has been purified from an extremely thermophilic bacterium, Thermus caldophilus GK24 [Taguchi, H., Yamashita, M., Matsuzawa, H. and Ohta, T. (1982) J. Biochem. ...

Heat-stable and fructose-1,6-bisphosphate-activated L-lactate dehydrogenase (EC 1.1.1.27) has been purified from an extremely thermophilic b …

7

Heat-stable and fructose 1,6-bisphosphate-activated L-lactate dehydrogenase from an extremely thermophilic bacterium.

Taguchi H, Yamashita M, Matsuzawa H, Ohta T. Taguchi H, et al. J Biochem. 1982 Apr;91(4):1343-8. doi: 10.1093/oxfordjournals.jbchem.a133821. J Biochem. 1982. PMID: 7096290 Free article.

8

Carboxypeptidase Taq, a thermostable zinc enzyme, from Thermus aquaticus YT-1: molecular cloning, sequencing, and expression of the encoding gene in Escherichia coli.

Lee SH, Taguchi H, Yoshimura E, Minagawa E, Kaminogawa S, Ohta T, Matsuzawa H. Lee SH, et al. Among authors: taguchi h. Biosci Biotechnol Biochem. 1994 Aug;58(8):1490-5. doi: 10.1271/bbb.58.1490. Biosci Biotechnol Biochem. 1994. PMID: 7765282 Free article.

9

Role of histidine 188 in fructose 1,6-bisphosphate- and divalent cation-regulated L-lactate dehydrogenase of Lactobacillus casei.

Taguchi H, Ohta T. Taguchi H, et al. Biosci Biotechnol Biochem. 1995 Mar;59(3):451-8. doi: 10.1271/bbb.59.451. Biosci Biotechnol Biochem. 1995. PMID: 7766183 Free article.

10

Essential role of arginine 235 in the substrate-binding of Lactobacillus plantarum D-lactate dehydrogenase.

Taguchi H, Ohta T. Taguchi H, et al. J Biochem. 1994 May;115(5):930-6. doi: 10.1093/oxfordjournals.jbchem.a124441. J Biochem. 1994. PMID: 7961609 Free article.

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