| Budget Amount *help |
¥14,170,000 (Direct Cost: ¥10,900,000、Indirect Cost: ¥3,270,000)
Fiscal Year 2014: ¥2,860,000 (Direct Cost: ¥2,200,000、Indirect Cost: ¥660,000)
Fiscal Year 2013: ¥2,860,000 (Direct Cost: ¥2,200,000、Indirect Cost: ¥660,000)
Fiscal Year 2012: ¥2,860,000 (Direct Cost: ¥2,200,000、Indirect Cost: ¥660,000)
Fiscal Year 2011: ¥5,590,000 (Direct Cost: ¥4,300,000、Indirect Cost: ¥1,290,000)
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| Outline of Final Research Achievements |
Pyridoxal 5'-phosphate (PLP) is an indispensable cofactor in many enzymes. The catalytic mechanism of the first part, from substrate binding to PLP to formation of quinonid intermediate, is characterized in several PLP enzymes, but the latter half is not fully understood. We determined X-ray structures of a series of reaction intermediates to elucidate the mechanism of PLP-dependent methionine γ-lyase. The structures reveal that the methionine degradation is carried out by aldimine-based C4'-Nα-Cα system, followed by proton migration from the Cα to C4' position. After releasing methanethiol, the latter half of intermediates suggest that the reaction processes leading to the releasing 2-aminobutyrate accounted for a concerted [1,5]-hydrogen sigmatropy with respect to the C4' and Cγ-carbon sites. Taken together, these structural intermediates successfully depicted overall reaction process of γ-elimination.
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