2011 Fiscal Year Final Research Report
Investigation of the structure and reaction mechanisms of human peptidylglycineα-amidating monooxygenase
| Project/Area Number |
21750181
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Chemistry related to living body
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| Research Institution | Kurume University |
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Principal Investigator |
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| Project Period (FY) |
2009 – 2011
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| Keywords | 酵素化学 |
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| Research Abstract |
Peptide C-terminalα-amide groups essential for the full biological activity of many peptide hormones are produced by a bifunctional peptidylglycineα-amidating enyme(PAM). PAM consists of peptidylglycineα-hydroxylating monooxygenase(PHM) and peptidylamidoglycolate lyase(PAL). The purposes of this study are the clarification of the roles of the metals in PAM for understanding its reaction mechanism. We prepared Apo-PAM/PAL and Metal(s)-substituted enzymes. Apo-enzymes are remarkably diminished the PHM and PAL activities. But the Cu-substituted PAM restored the PHM activity, the Zn-substituted PAL restored the PAL activity, and the Cu, Zn-substituted PAM fully restored the PAM(PHM and PAL) activity. In addition, the effects of a series of divalent metals on the PAM activity were determined. Based on the findings, we will discuss the roles of the enzyme-bound metals in the PAM reaction.
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