
永田 信治
- 学術論文 -
H.
Misono, H. Maeda, K. Tuda, S. Ueshima, N.
Miyazaki, S. Nagata.
Characterization
of an inducible phenylserine aldolase from Pseudomonas putida
24-1.
Appl. Environ. Microbiol., 71,
p.4602 (2005)
T.
Yamashita, M. Ashiuchi, K. Ohnishi, S. Kato, S.
Nagata, H.
Misono.
Molecular
identification of monomeric aspartate racemase from Bifidobacterium
bifidum.
Eur. J.
Biochem., 271,
p.4798 (2004)
E. K.
Chowdhury, Y. Akaishi,
S. Nagata, H.
Misono.
Cloning
and overexpression of the 3-hydroxyisobutyrate dehydrogenase gene from
Pseudomonas putida E23.
Biosci.
Biotechnol. Biochem., 67,
p.438 (2003)
R.
Katoh, S.
Nagata, H. Misono.
Cloning
and sequenceing of the leucine dehydrogenase gene from Bacillus
sphaericus IFO3525 and importance of the C-terminal region
for the
enzyme activity,
J. Mol.
Catalysis
B:Enzymatic, 23,
p.239 (2003)
R. Katoh, S.
Nagata, A. Ozawa, K. Ozawa, T.
Ohshima, M.
Kamekura, H. Misono.
Purification
and
characterization of
leucine dehydroganase from an alkalophlic halophile, Natronobacterium
magadii MS-31.
J.
Mol. Catalysis B:Enzymatic, 23, p.231
(2003)
S.
Nagata, Y.
Kobayashi, S. Shinkawa,
R. Katoh,
T. Ohshima, H. Misono.
Novel
halophilic 2-aminobutyrate dehydrogenase from Halobacterium
saccahrovorum DSM1137.
J.
Mol. Catalysis B:Enzymatic, 23,
p.223 (2003)
T.
Yamashita, M. Ashiuchi, K. Ohnishi, S. Kato, S. Nagata, H. Misono.
Molecular
characterization of alanine racemase from Bifidobacterium
bifidum.
J. Mol.
Catalysis B:Enzymatic, 23,
p.213 (2003)
H.
Fujisawa, S. Nagata,
H. Misono.
Characterization
of
short-chain dehydrogenase/reductase homologues of Escherichia
coli
(YdfG) and Saccharomyces cerevisiae (YMR226C).
Biochim.
Biophys. Acta, 1645,
p.89 (2003)
H.
Okuda, S. Nagata, H.
Misono.
Cloning,
equencing, and overexpression in Eshcerichia coli
of a phenylsaerin
dehydratase gene from Ralstonia pickettii PS22.
Biosci.
Biotechnol. Biochem., 66, p.2755
(2002)
H.
Fujisawa, S.
Nagata, E. K. Chowdhury, M.
Matsumoto, H.
Misono.
Cloning
and sequencing of the serine dehydrogenase gene from Agrobacterium
tumefaciens.
Biosci.
Biotechnol. Biochem., 66, p.1137
(2002)
T. Miyaji, M.
Ashiuchi, K. Packdibamrung, S. Nagata, and H.
Misono.
Characterization
of D-threonine dehydrogenase homologues of Escherichia coli,
YbbQ and
YhaE.
J. Mol. Catalysis B:
Enzymatic, 12,
p.77
(2001)
S. Sakamoto, M.
Seki, S.
Nagata, and H.
Misono.
Cloning,
sequencing, and expression of meso-diaminopimelate dehydrogenase gene
from Bacillus sphaericus.
J.
Mol. Catalysis B: Enzymatic, 12, p.85
(2001)
H. Uehigashi, R.
Katoh, O.
Kawamoto, M. Seki, E. Nakagawa, Y. Ojima, S. Nagata, H. Misono.
Breeding
of sake yeasts that produce enhanced levels of flavor by transformation
with a mutanted LEU4 gene or leudh
gene.
J.
Brew. Soc. Japan, 96, p.129
(2001)
T.
Shimamura, A. Takamori, H. Ukeda, S. Nagata, and M. Sawamura.
Relationship
between
the reduction
of tetrazolium salt XTT and DNA strand Breakage with aminosugars.
J.
Agric. Food Chem., 48,
p.1204 (2000)
H.
Uehigashi, H. Moriyama, H. Sugano, S. Nagata, H. Misono.
Effect
of
the
conditions used in
the steamed rice cooling process of sake brewing on aging.
J.
Brew.
Soc. Japan, 95,
p.70 (2000)
H. Uehigashi,
Y. Nakamura, H. Moriyama,
M. Mizobuchi, N. Sugano, S. Nagata, H. Misono.
The
Characterizations of the
Ginnoyume
Rice Cultivar for Sake Brewing.
J.
Brew.
Soc. Japan, 94, p.840
(1999)
H. Uehigashi, E.
Nakagawa,
H. Moriyama, S. Nagata, H. Misono.
Breeding
of sake yeast that produce
enhanced levels
of flavor by transformation with a mutated FAS2 gene and their
utilization in brewing rice flour shochu.
J.
Brew. Soc. Japan, 94, p.840
(1999)
E.
K. Chowdhury,
T. Saito, S.
Nagata, M. Ashiuchi, H. Misono.
Alanine
dehydrogenase from Enterobacter aerogenes:
Purification,
characterization, primary structure.
Biosci.
Biotech. Biochem., 62, p.2357
(1998)
M.
Ashiuchi,
K. Packdibamrung, T. Miyaji, S. Nagata, H. Misono.
Nucleotide
sequence, cloning, and
overexpression of the
D-threonine dehydrogenase gene from Pseudomonas cruciviae.
FEMS
Microbiol.
Lett.,167, p.75
(1998)
Ji-Quan
Liu, S.
Nagata, T.
Dairi, H. Misono. A. Shimizu , H. Yamada.
The
GLY1 gene of Saccharomyces
cerevisiae
encodes a low-specific L-threonine aldolase that catalyzes cleavage of
L-allo-threonine and L-threonine to glycine.
Eur.
J. Biochem., 245 p.289
(1997)
E.
K. Chowdhury,
I.
Higuchi, S. Nagata, H.
Misono.
A Novel
NADP-dependent
serine dehydrogenase
from
Agrobacterium tumefaciens.
Biosci.
Biotech. Biochem., 61,
p.152 (1997)
E.
K.
Chowdhury, S. Nagata, H. Misono.
3-Hydroxyisobutyrate
dehydrogenase from Pseudomonas putida E23:
Purification and
characterization.
Biosci.
Biotech. Biochem., 60, p.2043
(1996)
H.
Okuda, S.
Nagata,
H.Misono.
A novel
phenylserine
dehydratase
from Pseudomonas pickettii PS22: Purification,
characterization, and
sequence of its phosphopyridoxylpeptide.
J.
Biochem., 119, p.690
(1996)
H. Misono, H.
Okuda, K. Shin, S. Nagata, S.
Nagasaki.
Occerrence
of
an
Inducible Phenylserine Dehydratase in Pseudomonas pickettii
PS22
Isolated from Soil.
Biosci.
Biotech. Biochem., 59, p.339
(1995)
S.
Nagata, S.
Bakthavatsalam, A.G.
Galkin, H.
Asada, S. Sakai, N. Esaki, K. Soda, T. Ohshima, S. Nagasaki, H. Misono.
Gene
cloning,
purification, and characterization of thermostable and halophilic
leucinedehydrogenase from a halophilic thermophile, Bacillus
licheniformis TSN9.
Appl.
Microbiol. Biotechnol.,
44, p.4432 (1995)
- 特 許 -
出願日:平成15年2月17日、「新規な環状オリゴ糖生成酵素、その製造方法および環状イヌロオリゴ糖の製造方法」、発明者:南条文雄、永田信治、味園春雄、出願人:東京フードテクノ(株)、日本、特願2003-038182
出
願日:平成13年1月22日、公開日:平成14年7月30日、「(S)-4-ハロ-3-ヒドロキシ酪酸エステルの製造に有用な酵素をコードする遺伝子、そ
の取得方法、及びこれを利用した光学活性アルコールの製造方法」、発明者:山本浩明、永田信治、味園春雄、出願人:ダイセル化学(株)、日本、特開
2002-209592(P2002-209592A)
出願日:平成10年10月19日、公開日:平成12年5月9日、「アラニン脱水素酵素遺伝子、組換え体DNA及びアラニン脱水素酵素の製造法」、発明者:味園春雄、永田信治、鈴木英之、出願人:キッコーマン(株)、日本、特開2000
-125876(P2000-125876A)
村松 久司
村松久司、三原久明、栗原達夫、江崎信芳
N-アルキルアミノ酸と環状イミノ酸の不斉合成に利用できる酵素
月刊ファインケミカル、37(3)、p.12 (2008)
村松久司、三原久明、栗原達夫、江崎信芳
光学活性なN-アルキルアミノ酸および環状イミノ酸の生産に有用な酵素に関する研究
応用微生物学研究、4(2)、p.27 (2007)
Y.
Yamanishi, H. Mihara, M. Osaki, H. Muramatsu, N. Esaki, T. Sato, Y.
Hizukuri, S. Goto, M. Kanehisa.
Prediction of
missing enzyme genes in a bacterial metabolic network.
FEBS J. 274(9), p2262-2273
(2007)
M.
Yasuda, M. Ueda, H. Muramatsu, H. Mihara, N. Esaki.
Enzymatic
synthesis of cyclic amino acids by N-methyl-L-amino
acid dehydrogenase from Pseudomonas
putida.
TETRAHEDRON-ASYMMETRY.
17(12),
p.1775-1779 (2006)
H.
Muramatsu, H. Mihara, M. Yasuda, M. Ueda, T. Kurihara, N. Esaki.
Enzymatic
synthesis of L-pipecolic acid by Delta1-piperideine-2-carboxylate
reductase from Pseudomonas
putida.
Biosci.
Biotechnol. Biochem. 70(9),
p.2296-2298 (2006)
M.
Goto, H. Muramatsu, H. Mihara, T. Kurihara, N. Esaki, R. Omi, I.
Miyahara, K. Hirotsu.
Crystal
structure of
Delta1-piperideine-2-carboxylate/Delta1-pyrroline-2-carboxylate
reductase belonging to new family of NAD(P)H-dependent oxidoreductases
conformational change, substrate recognition, and stereochemistry of
the reaction.
J.
Biol. Chem. 280(49),
p.40875-40884 (2005)
H.
Muramatsu, H. Mihara, M. Goto, I. Miyahara, K. Hirotsu, T. Kurihara, N.
Esaki.
A new family of NAD(P)H-dependent
oxidoreductases distinct from conventional Rossmann-fold proteins.
J. Biosci. Bioeng. 99(6), p.541-547
(2005)
H.
Muramatsu, H. Mihara, R. Kakutani, M. Yasuda, M. Ueda, T. Kurihara, N.
Esaki.
The putative malate/lactate dehydrogenase
from Pseudomonas putida
is a NADPH-dependent
Delta1-piperideine-2-carboxylate/Delta1-pyrroline-2-carboxylate
reductase involved in the catabolism of D-lysine and D-proline.
J. Biol. Chem. 280(7), p.5329-5335
(2005)
H.
Mihara, H. Muramatsu, R. Kakutani, M. Yasuda, M. Ueda, T. Kurihara, N.
Esaki.
N-Methyl-L-amino
acid dehydrogenase from Pseudomonas
putida, a novel member of unusual NAD(P)-dependent
oxidoreductase superfamily.
FEBS J. 272(5), p.1117-1123
(2005)
H.
Muramatsu, H. Mihara, R. Kakutani, M. Yasuda, M. Ueda, T. Kurihara, N.
Esaki.
Enzymatic synthesis of N-methyl-L-phenylalanine
by a novel enzyme, N-methyl-L-amino
acid dehydrogenase, from Pseudomonas
putida.
TETRAHEDRON-ASYMMETRY.
15(18),
p.2841-2843 (2004)
Copyright(c)
2007 Laboratory of Applied Microbiology, Faculty of Agriculture, Kochi
University. All right reserved.