游动放线菌抗生素肽内酯酶的底物特异性
Substrate specificity of Actinoplanes antibiotic peptide lactonases.
作者信息
Perlman D, Hou C T
出版信息
Appl Microbiol. 1969 Aug;18(2):272-3. doi: 10.1128/am.18.2.272-273.1969.
Abstract
A constitutive peptide lactonase from Actinoplanes missouriensis hydrolyzed echinomycin, stendomycin, thiostrepton, vernamycin B, staphylomycin S, and etamycin. An induced lactonase hydrolyzed actinomycin but not the other peptide lactones.
摘要
来自密苏里游动放线菌的一种组成型肽内酯酶可水解棘霉素、链霉素、硫链丝菌素、维纳霉素B、葡萄球菌霉素S和埃他霉素。一种诱导型内酯酶可水解放线菌素，但不能水解其他肽内酯。
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本文引用的文献
1
2
Microbial transformations of peptide antibiotics. II. Site of actinomycin degradation in Actinoplanes missouriensis.肽类抗生素的微生物转化。II. 密苏里游动放线菌中放线菌素的降解位点。
Hindustan Antibiot Bull. 1968;10(4):269-73.
3
Microbial transformations of peptide antibiotics. I. Degradation of actinomycins by Actinoplanes species.肽类抗生素的微生物转化。I. 游动放线菌属菌种对放线菌素的降解
Antimicrob Agents Chemother (Bethesda). 1966;6:581-6.
4
Microbial metabolism of actinomycins and other heterodetic antibiotic peptides.放线菌素及其他杂肽抗生素的微生物代谢
Biochem Biophys Res Commun. 1966 Aug 23;24(4):513-8. doi: 10.1016/0006-291x(66)90349-4.
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