| Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2016: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2015: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2014: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Outline of Final Research Achievements |
Objectives To predict the amino acid residues playing important roles in acetyl-CoA and substrate binding and to study the acetyl group transfer mechanism in Chryseobacterium sp. strain 5-3B N-Acetyltransferase (5-3B NatA).
Results We constructed a 3-dimensional homology model of 5-3B NatA and compared the theoretical structure with the structures of previously reported proteins belonging to the bacterial GCN5 N-acetyltransferase family. Homology modeling of the 5-3B NatA structure and a characterization of its kinetic parameters identified the essential amino acid residues involved in binding and acetyl-group transfer. Thus, 126Leu, 132Leu, and 135Lys and 100Tyr and 131Lys were implicated in the binding of phosphopantothenic acid and adenosyl biphosphate, respectively. Both 83Glu and 133Tyr were suggested to catalyze acetyl-group transfer to L-2-phenylglycine.
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