Morino Y - Search Results

1

Pre-steady-state kinetics of Escherichia coli aspartate aminotransferase catalyzed reactions and thermodynamic aspects of its substrate specificity.

Kuramitsu S, Hiromi K, Hayashi H, Morino Y, Kagamiyama H. Kuramitsu S, et al. Among authors: morino y. Biochemistry. 1990 Jun 12;29(23):5469-76. doi: 10.1021/bi00475a010. Biochemistry. 1990. PMID: 2201406

2

The role of His143 in the catalytic mechanism of Escherichia coli aspartate aminotransferase.

Yano T, Kuramitsu S, Tanase S, Morino Y, Hiromi K, Kagamiyama H. Yano T, et al. Among authors: morino y. J Biol Chem. 1991 Apr 5;266(10):6079-85. J Biol Chem. 1991. PMID: 2007566 Free article.

3

Effects of replacement of tryptophan-140 by phenylalanine or glycine on the function of Escherichia coli aspartate aminotransferase.

Hayashi H, Inoue Y, Kuramitsu S, Morino Y, Kagamiyama H. Hayashi H, et al. Among authors: morino y. Biochem Biophys Res Commun. 1990 Mar 16;167(2):407-12. doi: 10.1016/0006-291x(90)92037-z. Biochem Biophys Res Commun. 1990. PMID: 2182010

4

Substitution of a lysyl residue for arginine 386 of Escherichia coli aspartate aminotransferase.

Inoue Y, Kuramitsu S, Inoue K, Kagamiyama H, Hiromi K, Tanase S, Morino Y. Inoue Y, et al. Among authors: morino y. J Biol Chem. 1989 Jun 5;264(16):9673-81. J Biol Chem. 1989. PMID: 2498335 Free article.

5

[Arg292----Val] or [Arg292----Leu] mutation enhances the reactivity of Escherichia coli aspartate aminotransferase with aromatic amino acids.

Hayashi H, Kuramitsu S, Inoue Y, Morino Y, Kagamiyama H. Hayashi H, et al. Among authors: morino y. Biochem Biophys Res Commun. 1989 Feb 28;159(1):337-42. doi: 10.1016/0006-291x(89)92443-1. Biochem Biophys Res Commun. 1989. PMID: 2564274

6

cDNA cloning and expression of pig cytosolic aspartate aminotransferase in Escherichia coli: amino-terminal heterogeneity of expressed products and lack of its correlation with enzyme function.

Nagashima F, Tanase S, Fukumoto Y, Joh T, Nomiyama H, Tsuzuki T, Shimada K, Kuramitsu S, Kagamiyama H, Morino Y. Nagashima F, et al. Among authors: morino y. Biochemistry. 1989 Feb 7;28(3):1153-60. doi: 10.1021/bi00429a033. Biochemistry. 1989. PMID: 2653435

7

Determination of human aspartate aminotransferase isoenzymes by their differential sensitivity to proteases.

Teranishi H, Morino Y, Nishino T, Murao S, Yagi T, Kagamiyama H, Harada N. Teranishi H, et al. Among authors: morino y. Clin Biochem. 1988 Dec;21(6):347-52. doi: 10.1016/s0009-9120(88)80015-8. Clin Biochem. 1988. PMID: 3069246

8

Role of Asp222 in the catalytic mechanism of Escherichia coli aspartate aminotransferase: the amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal 5'-phosphate.

Yano T, Kuramitsu S, Tanase S, Morino Y, Kagamiyama H. Yano T, et al. Among authors: morino y. Biochemistry. 1992 Jun 30;31(25):5878-87. doi: 10.1021/bi00140a025. Biochemistry. 1992. PMID: 1610831

The presteady-state reactions of these two mutant enzymes with [2-2H]aspartate revealed a deuterium isotope effect (kH/kD = 6.0) greater than that [kH/kD = 2.2; Kuramitsu, S., Hiromi, K., Hayashi, H., Morino, Y., & Kagamiyama, H. (1990) Biochemistry 29, 5469-547 …

The presteady-state reactions of these two mutant enzymes with [2-2H]aspartate revealed a deuterium isotope effect (kH/kD = 6.0) greater tha …

9

Tyr225 in aspartate aminotransferase: contribution of the hydrogen bond between Tyr225 and coenzyme to the catalytic reaction.

Inoue K, Kuramitsu S, Okamoto A, Hirotsu K, Higuchi T, Morino Y, Kagamiyama H. Inoue K, et al. Among authors: morino y. J Biochem. 1991 Apr;109(4):570-6. doi: 10.1093/oxfordjournals.jbchem.a123421. J Biochem. 1991. PMID: 1869510 Free article.

10

Mammalian aspartate aminotransferase isozymes. From DNA to protein.

Morino Y, Shimada K, Kagamiyama H. Morino Y, et al. Ann N Y Acad Sci. 1990;585:32-47. doi: 10.1111/j.1749-6632.1990.tb28039.x. Ann N Y Acad Sci. 1990. PMID: 2192615 No abstract available.

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