1987 Fiscal Year Final Research Report Summary
Bilogical Roles on N-Acylamino Acid Releasing-enzyme-especially on the protein myristylation-
| Project/Area Number |
61580144
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
物質生物化学
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| Research Institution | Osaka University |
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Principal Investigator |
TSUNASAWA Susumu Associate professor, Institute for Protein Research, Osaka University, 蛋白質研究所, 助教授 (30029962)
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| Co-Investigator(Kenkyū-buntansha) |
YAMADA Michiyuki Associate professor, Institute for Protein Research, OsakaUniversity, 蛋白質研究所, 助教授 (10076995)
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| Project Period (FY) |
1986 – 1987
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| Keywords | Acylamino acid releasing-enzyme / ミリスチル化 |
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| Research Abstract |
To elucidate the biological roles on N-acylamino acid releasing-enzyme, its substrate specificity was at first studied with acetylmethionyl amino acids, acetylalanyl peptides ranging from dithrough penta-alanine, and N-acylmethionylalanine having various acyl groups, and the following results were thus found. 1) The enzyme hydrolyses all the peptides tested except for acetyl-L-methionuyl-L-proline, -L-aspartic acid and -D-amino acids. 2) Among acetylated derivatives of oligoalanine, acetyl di- and trialanine were most rapidly hydrolyzed by the enzyme. 3) The enzyme removes more effectively acetyl or propionyl amino acid from various N-acylated peptides. As the second step, the determination of the primary structure of the enzyme was tried. Amino acid sequences of several peptides generated from the enzyme from pig liver, by digestion with Achromobacter protease I were partially determined, and the isolation of cDNA encoding the enzyme has been now performing in the cDNA library constructed from pig liver using a 24-mer nucleotide corresponding to the sequence partially determined as above, Glu-Pro-Glu-Glu-Ala-Ala-Ala-Leu-Tyr, as a prove.
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