Structure and reaction mechanism analyses of enzymes in an alternative menaquinone biosynthetic patyway
| Project/Area Number |
24780097
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Applied biochemistry
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| Research Institution | Shinshu University |
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Principal Investigator |
ARAI Ryoichi 信州大学, 学術研究院繊維学系, 助教 (50344023)
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| Project Period (FY) |
2012-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2014: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2013: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2012: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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| Keywords | メナキノン / ビタミンK / 生合成 / 酵素反応機構 / X線結晶構造解析 / MqnD / 高度好熱菌 / ピロリ菌 / DHNA synthase / 結晶中酵素反応 / 酵素 / 反応機構 / 構造生物学 / 酵素化学 / Ｘ線結晶構造解析 |
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| Outline of Final Research Achievements |
An alternative biosynthetic pathway of menaquinone (vitamin K2) was found in some microorganisms including Streptomyces coelicolor and Thermus thermophilus. Since the pathogenic species such as Helicobacter pylori and Campylobacter jejuni also have essential enzymes in the alternative menaquinone biosynthetic pathway, the enzymes are attractive targets for the development of chemotherapeutics. Here we report the 1.5 angstrom crystal structure of the H145A variant of MqnD from T. thermophiles, complexed with its substrate. The substrate with ring-closing form was bound to the active-site pocket between the two domains, a large domain and a small domain. The His145Ala variant produces no enzymatic reaction, suggesting that His145 is an essential active residue as a catalytic base. Furthermore, we solved the crystal structure of MqnD complexed with the product, one of its reaction products. These results provide new insights into the enzymatic reaction mechanism of MqnD.
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Report
(5 results)
Research Products
(85 results)
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[Journal Article] Molecular cloning, gene expression analysis, and recombinant protein expression of novel silk proteins from larvae of a retreat-maker caddisfly, Stenopsyche marmorata2015
Author(s)
Xue Bai, Mayo Sakaguchi, Yuko Yamaguchi, Shiori Ishihara, Masuhiro Tsukada, Kimio Hirabayashi, Kousaku Ohkawa, Takaomi Nomura, Ryoichi Arai
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Journal Title
Biochemical and Biophysical Research Communications
Volume: 464
Issue: 3
Pages: 814-819
DOI
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
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[Presentation] A De Novo Heme Protein, Dnhps1, Created from a 5-Amino Acid Alphabet
Author(s)
Fukuda, S., Kurasawa, S., and Arai, R.
Organizer
27th Annual Symposium of The Protein Society
Place of Presentation
Boston Marriott Copley Place, Boston, MA, USA
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[Presentation] Molecular cloning of novel silk proteins from larvae of caddisfly, Stenopsyche marmorata.
Author(s)
X. Bai, K. Ohkawa, T.Nomura, S. Ishihara, Y. Yamaguchi, M. Tsukada, K. Abe, K. Hirabayashi, R. Arai
Organizer
The 8th China International Silk Conference
Place of Presentation
蘇州大学 (Suzhou, China)
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[Presentation] Arai, R., Matsuo, K. and Dairi, T.
Author(s)
Crystal structures of MqnD, a menaquinone biosynthetic enzyme, complexed with the product, 1,4-dihydroxy-6-naphthoate, and its analogs
Organizer
4th International Symposium on Diffraction Structural Biology (ISDSB 2013)
Place of Presentation
名古屋市中小企業振興会館（名古屋）
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