Yoshida S, Nakamura Y, Naganawa H, Aoyagi T, Takeuchi T
Institute of Microbial Chemistry, Tokyo, Japan.
J Antibiot (Tokyo). 1990 Feb;43(2):149-53. doi: 10.7164/antibiotics.43.149.
Probestin, a new inhibitor of aminopeptidase M, has been isolated from the culture broth of Streptomyces azureus MH663-2F6. The 1H and 13C NMR studies and amino acid analysis confirmed the presence of one 3-amino-2-hydroxy-phenylbutanoic acid, leucine and two proline residues in the molecule. Stereochemistries of these amino acids were determined by HPLC analysis. The fragmentation pattern shown in the mass spectrum and the chemical analysis on probestin clarified the amino acid sequence. Thus the structure of probestin was defined as (2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl-L-leucyl-L-prolyl-L-pro line.
脯氨菌素是一种新型氨肽酶M抑制剂,已从天蓝链霉菌MH663 - 2F6的培养液中分离出来。1H和13C核磁共振研究以及氨基酸分析证实该分子中存在一个3 - 氨基 - 2 - 羟基 - 苯基丁酸、亮氨酸和两个脯氨酸残基。这些氨基酸的立体化学结构通过高效液相色谱分析确定。脯氨菌素质谱中显示的裂解模式和化学分析明确了氨基酸序列。因此,脯氨菌素的结构被定义为(2S,3R)-3 - 氨基 - 2 - 羟基 - 4 - 苯基丁酰基 - L - 亮氨酰基 - L - 脯氨酰基 - L - 脯氨酸。