Morino Y - Search Results

1

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.

2

Structural and functional role of the amino-terminal region of porcine cytosolic aspartate aminotransferase. Catalytic and structural properties of enzyme derivatives truncated on the amino-terminal side.

Fukumoto Y, Tanase S, Nagashima F, Ueda S, Ikegami K, Morino Y. Fukumoto Y, et al. Among authors: morino y. J Biol Chem. 1991 Mar 5;266(7):4187-93. J Biol Chem. 1991. PMID: 1999412 Free article.

3

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.

4

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

5

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

6

[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

7

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

8

Import and processing of precursor to mitochondrial aspartate aminotransferase. Structure-function relationships of the presequence.

Nishi T, Nagashima F, Tanase S, Fukumoto Y, Joh T, Shimada K, Matsukado Y, Ushio Y, Morino Y. Nishi T, et al. Among authors: morino y. J Biol Chem. 1989 Apr 15;264(11):6044-51. J Biol Chem. 1989. PMID: 2703479 Free article.

The precursor protein of pig mitochondrial aspartate aminotransferase (pre-mAspAT) contains a 29-residue presequence (Joh, T., Nomiyama, H., Maeda, S., Shimada, K., and Morino, Y. (1985) Proc. Natl. Acad. Sci. U. S. A. 82, 1-5). Pre-mAspAT produced in an in vitro tr …

The precursor protein of pig mitochondrial aspartate aminotransferase (pre-mAspAT) contains a 29-residue presequence (Joh, T., Nomiyama, H., …

9

Rat cytosolic aspartate aminotransferase: molecular cloning of cDNA and expression in Escherichia coli.

Horio Y, Tanaka T, Taketoshi M, Nagashima F, Tanase S, Morino Y, Wada H. Horio Y, et al. Among authors: morino y. J Biochem. 1988 May;103(5):797-804. doi: 10.1093/oxfordjournals.jbchem.a122349. J Biochem. 1988. PMID: 3053674 Free article.

10

Substitution of an arginyl residue for the active site lysyl residue (Lys258) of aspartate aminotransferase.

Kuramitsu S, Inoue Y, Tanase S, Morino Y, Kagamiyama H. Kuramitsu S, et al. Among authors: morino y. Biochem Biophys Res Commun. 1987 Jul 31;146(2):416-21. doi: 10.1016/0006-291x(87)90545-6. Biochem Biophys Res Commun. 1987. PMID: 3113421

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