Adriaens P, Meesschaert B, Wuyts W, Vanderhaeghe H, Eyssen H
Antimicrob Agents Chemother. 1975 Dec;8(6):638-42. doi: 10.1128/AAC.8.6.638.
Cultures of Penicillium chrysogenum, growth with [(35)S]sulfate or labeled amino acids, were examined by ion-exchange chromatography for possible peptidic precursors of penicillin. A sulfur-containing compound, present in both the mycelial extracts and the culture filtrates, was eluted at the location of the synthetic lld-tripeptide delta-(l-alpha-aminoadipyl)-l-cysteinyl-d-valine. Since this compound was also labeled when the cultures were incubated with dl-[6-(14)C]alpha-aminoadipic acid, l-[3,3'-(3)H]cystine, or dl-[1-(14)C]valine, its identity with the synthetic lld-tripeptide can be accepted. No delta-(l-alpha-aminoadipyl)-l-cysteine or lll-tripeptide were detected. The implications of these findings for tripeptide and penicillin biosynthesis are discussed.
用离子交换色谱法对产黄青霉培养物(用[35S]硫酸盐或标记氨基酸培养)进行检测,以寻找青霉素可能的肽类前体。在菌丝提取物和培养滤液中均存在一种含硫化合物,其洗脱位置与合成的lld-三肽δ-(l-α-氨基己二酰基)-l-半胱氨酰基-d-缬氨酸相同。由于当培养物与dl-[6-(14)C]α-氨基己二酸、l-[3,3'-(3)H]胱氨酸或dl-[1-(14)C]缬氨酸一起孵育时该化合物也被标记,因此可以认为它与合成的lld-三肽是同一物质。未检测到δ-(l-α-氨基己二酰基)-l-半胱氨酸或lll-三肽。讨论了这些发现对三肽和青霉素生物合成的意义。