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発表論文リスト
[2012年度 宮崎大学着任以降〜]
・Atomic-resolution structure of the phycocyanobilin:ferredoxin
oxidoreductase I86D mutant in complex with fully protonated biliverdin.
Y. Hagiwara, K. Wada, T. Irikawa, H. Sato, M. Unno, K. Yamamoto, K.
Fukuyama, M. Sugishima.
FEBS Lett., 590, 3425-3434 (2016) (2014年IF: 3.169)
・Phosphonate-based irreversible inhibitors of human
γ-glutamyltranspeptidase (GGT).
GGsTop is a non-toxic and highly selective inhibitor with critical
electrostatic
interaction with an active-site residue Lys562 for enhanced inhibitory
activity.
A. Kamiyama, M. Nakajima, L. Han, K.Wada, M. Mizutani. Y. Tabuchi,
A. Kojima,
I. Matsui, H. Suzuki, K. Fukuyama, B. Watanabe, J. Hiratake.
Bioorg. & Med. Chem., 24, 5340-5352, 2016 (2014年IF: 2.420)
・ビリン還元酵素PcyAと基質ビリベルジン複合体の中性構造解析から見えてきたもの"
海野昌喜、日下勝弘、玉田太郎、杉島正一、和田 啓、萩原義徳、福山恵一
日本中性子科学会誌「波紋」、26, 130-134 (2016)
・ Functional Dynamics Revealed by the Structure of the SufBCD Complex,
a Novel ATP-binding Cassette (ABC) Protein That Serves as a Scaffold
for Iron-Sulfur Cluster Biogenesis.
K. Hirabayashi, E. Yuda, N. Tanaka, S, Katayama, K, Iwasaki, T.
Matsumoto, G. Kurisu, F. W. Outten, K. Fukuyama, Y. Takahashi, K.
Wada*
J. Biol. Chem, 290, 29717-29731, Dec 11, 2015 (2014年IF: 4.573)
・光合成色素フィコシアノビリンを合成する酵素と基質ビリベルジンとの複合体の中性子結晶解析
福山 恵一、和田 啓、杉島 正一、海野 昌喜 、生化学, 87(6): 753-757 (2015)
・中性子結晶構造解析で明らかになったビリン還元酵素PcyA基質複合体の二つの水素化状態と構造的特徴
海野 昌喜, 杉島 正一、和田 啓、萩原 義徳、日下 勝弘、玉田 太郎、福山 恵一 、日本結晶学会誌、57, 297-303
(2015)
・Insights into the Proton Transfer Mechanism of a Bilin Reductase PcyA
Following Neutron Crystallography.
・M. Unno,, K. Ishikawa-Suto, K. Kusaka, T. Tamada, Y. Hagiwara, M.
Sugishima, K. Wada , T. Yamada, K. Tomoyori, T. Hosoya, I.
Tanaka, N. Niimura, R. Kuroki, K. Inaka, M. Ishihara, K. Fukuyama.
J. Am. Chem. Soc, 137, 5452-5460. Apr, 2015 (2014年IF: 12.113)
・The crystal structure of isoniazid-bound KatG catalase-peroxidase from
Synechococcus elongatus PCC7942. [雑誌表紙に採択]
S. Kamachi, K. Hirabayashi, M. Tamoi, S. Shigeoka, T. Tada, K. Wada*
FEBS Journal. 281, 54-64, Jan, 2015
(2013年IF:3.986: Biochemistry & Molecular Biology 分野で85/291番目)
・The 2.2 Â resolution structure of the catalase-peroxidase KatG from
Synechococcus elongatus PCC7942.
S. Kamachi, K. Wada*, M. Tamoi, S. Shigeoka, T. Tada*
Acta. Cryst. F. Structural biology communications, 70, 288-293, Mar.
2014.
(2012年IF:0.552:Crystallogpraphy分野で 17/23番目)
・Structural basis for the electron transfer from an open form of
NADPH-cytochrome P450 oxidoreductase to heme oxygenase.
M. Sugishima, H. Sato, Y. Higashimoto, J. Harada, K. Wada, K.
Fukuyama, M. Noguchi.
Proc. Natl. Acad. Sci. USA, 111, 2524-2529, Feb, 2014（2012年IF：9.737）
・Structure of Bacillus subtilis γ-glutamyltranspeptidase in complex
with acivicin: diversity of the binding mode of a classical and
electrophilic active-site directed glutamate analogue.
T. Ida, H. Suzuki, K. Fukuyama, J. Hiratake, K. Wada*
70, 607-614, Jan. 2014
(2012年IF:14.103: Biophysics分野で 1/72番目; Crystallography 分野で1/23番目;
BIOCHEMICAL RESEARCH METHODS 分野で2/75番目; Biochemistry & Molecular
Biology 分野で7/290番目)
・Glutathione-analogous peptidyl phosphorus esters as mechanism-based
inhibitors of γ-glutamyl transpeptidase for probing cysteinyl-glycine
binding site.
Bioinorg. Med. Chem. 22, 1176-1194, Dec. 2013.（2012年IF：2.903）
・γ-グルタミルトランスペプチダーゼの立体構造と特異的反応、 福山 恵一、和田 啓 、日本結晶学会誌、55, 340-344
(2013)[総説]
・Thermal denaturation and renaturation of γ-glutamyltranspeptidase of Escherichia
coli.
Thao Van Ho, Kaeko Kamei, Wada, K., Keiichi Fukuyama, and
Hideyuki Suzuki.
Biosci. Biotechnol. Biochem.77, 409-412, Feb. 2013 （2012年IF：1.292）.
・Structure-function relationships of ferredoxin-dependent bilin
reductases in "An integrating approach to photo functional hybrid
materials for energy and environment"
[ハードカバー著書表紙に採択]
Unno, M., Sugishima, M., Wada, K. and Fukuyama, K.
Nova Science Publishers, June 2013, 47-68. [著書]
・Establishment of a Bacterial Expression System andImmunoassay Platform
for the Major Capsid Protein of HcRNAV, a Dinoflagellate- Infecting RNA
Virus. Microbes Environ.
Wada, K., Kimura, K., Hasegawa, H., Fukuyama., K and
Nagasaki, K.
Microbes Environ., 27, 483-489, Oct. 2012 (2012年 IF; 2.444).
・γ-Glutamyltranspeptidase and Its Precursor in "Handbook of Proteolytic
Enzymes 3"
Hiratake,J., Suzuki,H., Fukuyama,K.,Wada, K. and Kumagai H.
Massachusetts, Academic Press, Dec. 2012, Chapter 820, 3714-3720.[著書]
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[2011年度以前の業績]
・A Simple and Large Scale Over-Expression Method for Carbon Monoxide
Dehydrogenase II from Thermophilic Bacterium Carboxydothermus
hydrogenoformans.
Inoue, T., Yoshida, T., Wada, K., Daifuku, T., Fukuyama, K. and
Sako, Y.
Biosci. Biotech. Biochem., 75, 1392-1394 (2011)
・Expression, purification and preliminary X-ray crystallographic
analysis of cyanobacterial biliverdin reductase.
Watanabe, A., Hirata, K., Hagiwara, Y., Yutani, Y., Sugishima, M.,
Yamamoto, M., Fukuyama, K., and Wada K.*
Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun., F67, 313-317
(2011).
・鉄硫黄クラスター生合成マシナリーの構造と作動機構
和田啓, 福山恵一, 高橋康弘.
化学と生物, Vol48, No.12, 831-838 (2010)
・One residue substitution in PcyA leads to unexpected changes in
tetrapyrrole substrate binding.
Wada, K., Hagiwara, Y., Yutani, Y. and Fukuyama, K.
Biochem. Biophys. Res. Commun., 402, 373-377 (2010).
・Enhancement of glutaryl-7-aminocephalosporanic acid acylase activity
of gamma-glutamyltranspeptidase of Bacillus subtilis.
Suzuki,H., Yamada, C., Kijima, K., Ishihara, S., Wada, K.,
Fukuyama, K., and Kumagai, H.
Biotechnol J., 5, 829-837 (2010).
・鉄硫黄クラスター生合成マシナリーの構造生物学
和田啓*
日本結晶学会誌, 52, 174-183 (2010).
・超分子マシナリーが担う鉄硫黄クラスターの生合成
高橋康弘、和田啓、福山恵一
生化学, Vol 82, no.2, 139-142 (2010).
・Crystal structure of the halotolerant γ-glutamyltranspeptidase from Bacillus
subtilis in complex with glutamate reveals its unique architecture
of the solvent-exposed catalytic pocket. [雑誌表紙に採択]
Wada, K., Irie, M., Suzuki, H. and Fukuyama, K.
FEBS J., 277, 100-1009 (2010).
・Molecular Dynamism of Fe-S Cluster Biosynthesis Implicated by the
Structure of the SufC2-SufD2 Complex.[雑誌表紙に採択]
Wada, K., Sumi, N., Nagai, R., Iwasaki, K., Sato,
T., Suzuki, K., Hasegawa, Y., Kitaoka, S., Minami, Y., Outten, W., F.,
Takahashi, Y. and Fukuyama, K.
J. Mol. Biol., 387, 245-258 (2009)
・γ-グルタミルトランスペプチダーゼの立体構造に基づいた成熟化と酵素反応機構
鈴木秀之、和田啓、福山恵一
蛋白質核酸酵素, Vol.54, No.3, 245-251 (2009).
・γ-グルタミルトランスペプチダーゼはどのように成熟化し、反応を触媒するか？
和田啓、鈴木秀之、福山恵一
日本応用酵素協会誌, No.43, 23-31 (2009).
・γ-グルタミルトランスペプチダーゼのグルタリル-7-アミノセファロスポラン酸アシラーゼへの変換-立体構造に基づく効果的変異導入
鈴木秀之、和田啓、福山恵一
バイオサイエンスとインダストリー、Vol.66, No.12, 660-666 (2008).
・The asymmetric trimeric architecture of [2Fe-2S] IscU: Implications
for its scaffolding during iron-sulfur cluster biosynthesis.
Shimomura, Y., Wada, K., Fukuyama, K. and Takahashi, Y.
J. Mol. Biol., 383, 133-143 (2008).
・Crystal Structures of Escherichia coli γ-Glutamyltranspeptidase in
Complex with Azaserine and Acivicin: Novel Mechanistic Implication for
Inhibition by Glutamine Antagonists. [雑誌表紙に採択]
Wada, K., Hiratake J, Irie M, Okada T, Yamada C,
Kumagai H, Suzuki H, Fukuyama K.
J. Mol. Biol., 380, 361-372 (2008).
・Improvement of Glutaryl-7-aminocephalosporanic Acid Acylase Activity
of Bacterial γ-Glutamyltranspeptidase.
Yamada, C., Kijima, K., Ishihara, S., Miwa, C., Wada, K.,
Okada, T., Fukuyama, K., Kumagai, H. and Suzuki, H.
Appl. Environ. Microbiol.. 74, 3400-3409 (2008).
・Crystal Structures of CbiL, a Methyltransferase Involved in Anaerobic
Vitamin B12 Biosynthesis, and its Complex with S-Adenosylhomocysteine:
Implications for the Reaction Mechanism.
Wada, K.*, Harada, J., Yaeda, Y., Tamiaki, H.,
Oh-oka, H and Fukuyama., K.
FEBS Journal, 274, 563-573 (2007).
・Crystal structure of the γ-glutamyltranspeptidase precursor protein
from Escherichia coli. Structural changes upon autocatalytic processing
and implications for the maturation mechanism.
Okada, T., Suzuki, K., Wada, K., Kumagai, H and Fukuyama, K.
J. Biol. Chem., 288, 2433-2439 (2007).
・Crystal structures of γ-glutamyltranspeptidase from Escherichia coli,
a key enzyme in glutathione metabolism, and its reaction intermediate.
Okada, T., Suzuki, H., Wada, K., Kumagai, H. and Fukuyama, K.
Proc. Natl. Acad. Sci. USA., 103, 6471-6476 (2006).
・Structure of apo-glyceraldehyde-3-phosphate dehydrogenase from
Synechococcus PCC7942.
Kitatani, T., Nakamura, Y., Wada, K., Kinoshita, T., Tamoi, M.,
Shigeoka, S. and Tada. T.
Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun.,62, 727-730
(2006)
・Crystal Structures of BchU, a Methyltransferase Involved in
Bacteriochlorophyll c Biosynthesis, and its Complex with
S-Adenosylhomocysteine: Implications for Reaction Mechanism.
Wada, K., Yamaguchi, H., Harada, J., Niimi, K.,
Osumi, S., Saga, Y., Oh-oka, H., Tamiaki, H. and Fukuyama, K.
J. Mol. Biol., 360, 839-849 (2006).
・Structure of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase
from Synechococcus PCC7942 complexed with NADP.
Kitatani, T., Nakamura, Y., Wada, K., Kinoshita, T., Tamoi, M.,
Shigeoka, S. and Tada. T.
Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun., 62, 315-319
(2006).
・Crystal structure of Escherichia coli SufC, an ABC-type ATPase
component of the SUF iron-sulfur cluster assembly machinery.
Kitaoka, S., Wada, K., Hasegawa, Y., Minami, Y., Fukuyama, K.
and Takahashi, Y.
FEBS Lett., 580, 137-143 (2006).
・Crystal structure of Escherichia coli SufA involved in biosynthesis of
iron-sulfur clusters: implications for a functional dimer. [雑誌表紙に採択]
Wada, K., Hasegawa, Y., Gong, Z., Minami, Y.,
Fukuyama, K. and Takahashi, Y.
FEBS Lett., 579, 6543-6548 (2005).
・dentification of variant molecules of Bacillus thermoproteolyticus
ferredoxin: crystal structure reveals bound coenzyme A and an
unexpected [3Fe-4S] cluster associated with a canonical [4Fe-4S] ligand
motif.
Shirakawa, T., Takahashi, Y., Wada, K., Hirota, J., Takao, T.,
Ohmori, D. and Fukuyama, K.
Biochemistry, 44, 12402-12410 (2005).
・Crystallization and preliminary X-ray diffraction study of BchU, a
methyltransferase from Chlorobium tepidum involved in
bacteriochlorophyll c biosynthesis.
Harada, J., Wada, K., Yamaguchi, H., Oh-oka, H., Tamiaki, H.
and Fukuyama, K.
Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun., 61, 712-714
(2005).
・Structural basis for thermostability of endo-1,5-alpha-L-arabinanase
from Bacillus thermodenitrificans TS-3.
Yamaguchi, A., Tada, T., Wada, K., Nakaniwa, T., Kitatani, T.,
Sogabe, Y., Takao, M., Sakai, T. and Nishimura, K.
J. Biochem., 137, 587-592 (2005).
・Crystal structure of chloroplastic ascorbate peroxidase from tobacco
plants and structural insights for its instability.
Wada, K.*, Tada, T., Nakamura, Y., Ishikawa, T.,
Yabuta, Y., Yoshimura, K., Shigeoka, S. and Nishimura, K.
J. Biochem., 134, 239-244 (2003).
・Crystallization and preliminary X-ray diffraction analysis of
chloroplastic ascorbate peroxidase from tobacco plants.
Wada, K.*, Tada, T., Nakamura, Y., Yoshimura, K.,
Shigeoka, S. and K. Nishimura.
Acta Crystallograph. Sect. D Struct. Biol. Cryst. Commun., D58,
559-561(2002).
・Crystallization and preliminary X-ray diffraction studies of
catalase-peroxidase from Synechococcus PCC 7942.
Wada, K.*, Tada, T., Nakamura, Y., Kinoshita, T.,
Tamoi, M., Shigeoka S. and Nishimura, K.
Acta Crystallograph. Sect. D Struct. Biol. Cryst. Commun.,D58, 157-159
(2002).
・Characterization of monoclonal antibodies against ascorbate peroxidase
isoenzymes: purification and epitope-mapping using immunoaffinity
column choromatography.
Yoshimura, Y., Ishikawa, T., Wada, K., Takeda, T., Kamata, Y.,
Tada, T., Nishimura, K., Nakano, Y. and Shigeoka, S.
Biochim. Biophys. Acta,1526, 168-174 (2001).
・Crystallization and preliminary X-ray analysis of a novel pectolytic
enzyme, polymethoxygalacturonase SX1 from Trichosporon penicillatum.
Tada, T., Lu, C, -T., Nakamura, Y., Wada, K., Katsuya, Y. and
Nishimura, K.
Acta Crystallograph. Sect. D Struct. Biol. Cryst. Commun., D57, 457-458
(2001).
・Crystallization and preliminary X-ray diffraction analysis of
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase of
Synechococcus PCC 7942.
Nakamura, Y., Tada, T., Wada, K., Kinoshita. T., Tamoi, M.,
Shigeoka, S. and Nishimura, K.
Acta Crystallograph. Sect. D Struct. Biol. Cryst. Commun., D57, 879-881
(2001).
・Purification, crystallization and preliminary X-ray diffraction
analysis of the fructose-1,6-/sedoheptulose-1,7-bisphosphatase of
Synechococcus PCC 7942.
Nakamura, Y., Tada, T., Wada, K., Kinoshita, T., Tamoi, M.,
Shigeoka, S., and Nishimura, K.
Acta Crystallograph. Sect. D Struct. Biol. Cryst. Commun., D57, 454-456
(2001).
・Crystallization and preliminary X-ray analysis of
endopolygalacturonase SE1 from Trichosporon, penicillatum.
Lu, C, -T., Tada, T., Nakamura, Y., Wada, K., Nishimura, K.,
Katsuya, Y., Sawada, M. and Sakai, Y.
Acta Crystallograph. Sect. D Struct. Biol. Cryst. Commun., D56,
1668-1669 (2000).
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