Biosynthesis of peptide inhibitor MR-387 by Streptomyces neyagawaensis：（生物合成肽抑制剂- 387先生的链霉菌属neyagawaensis）.pdfVIP

Biotechnology Letters, Vol 19, No 7, July 1997, pp. 607–610 11111 2 Biosynthesis of peptide inhibitor MR-387 3 4 by Streptomyces neyagawaensis 5 6 7 Myung-Chul Chung, Choong-Hwan Lee, Ho-Jae Lee, Yung-Hee Kho 8 and Hyo-Kon Chun 9 Enzyme Inhibition Research Unit, Korea Research Institute of Bioscience and Biotechnology (KRIBB), KIST, 10111 P.O. Box 115, Yusong, Taejon 305–600, Korea 1 2 Biosynthesis of MR-387 by Streptomyces neyagawaensis SL-387 was studied by testing the incorporation of radio- 3 active precursors and the detection of biosynthetic enzyme. L-Phenylalanine, L-valine, L-proline, and acetic acid were 4 efficiently incorporated into MR-387, but phenylethylamine and oxalic acid were not. These results suggest that the 5 (2S,3R)-3-amino-2-hydroxy-4-phenylbutanoic acid moiety of MR-387 is synthesized from phenylalanine and acetic 6 acid but not directly via the phenylethylamine. Synthesis of MR-387 is mediated by a peptide synthetase with a novel 7 activity. 8 9 20111 1 24 pts min base to base from Key words to line 1 of text 2 3 4 Introduction that the biosynthesis of the AHPA moiety of MR-387 5 MR-397A and B are peptide inhibitors of aminopepti- is not directly via the phenylethylamine converted by 6 dase N with the structures of (2S,3R)-3-amino-2- decarboxylation of phenylalanine which is mediated 7 hydroxy-4-phenylbutanoyl-L-valyl-L-prolyl-(2,4-trans)- by a phenylalanine decarboxylase. 8 L-hydroxy-proline and (2S,3R)-3-amino-2-hydroxy-4- 9 phenylbutanoyl-L