2010 Fiscal Year Final Research Report
Analyses of molecular mechanisms of homeostasis by carnosine in mammals and carnosine-hydrolyzing enzyme, CNDP2
| Project/Area Number |
20570132
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Functional biochemistry
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| Research Institution | Osaka University |
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Principal Investigator |
OKUMURA Nobuaki Osaka University, 蛋白質研究所, 准教授 (20224173)
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| Project Period (FY) |
2008 – 2010
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| Keywords | ペプチド / ペプチダーゼ / 立体構造 / ホメオスタシス |
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| Research Abstract |
Carnosine (beta-alanyl-L-histidine) is a dipeptide present at high concentrations in mammalian muscles and brain. Carnosine has been suggested to be ace as an antioxidant, but its function as well as the enzymes responsible for its synthesis and degradation has not well been understood. We have previously found an enzyme that can hydrolyze carnosine (CNDP2), and then in the present study, we have analyzed the structure, function and distrubution of CNDP2. We have determine the crystal structure of CNDP2 and revealed its structural features. In addition, we have found that it is highly expressed in the histaminergic neurons in the hypothalamus, raising a possibility that carnosine and CNDP2 may contribute the production of substrate for histamine synthesis.
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Research Products
(13 results)
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[Journal Article] Structural basis for substrate recognition and hydrolysis by mouse carnosinase CN2.2008
Author(s)
Unno, H., Yamashita, T., Ujita, S., Okumura N., Otani, H., Okumura, A., Nagai K., Kusunoki, M.
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Journal Title
J Biol Chem 283
Pages: 27289-99
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