Post-translational modification of polyketide and nonribosomal peptide synthases.
Post-translational modification of polyketide and nonribosomal peptide synthases.
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DOI：
10.1016/s1367-5931(97)80067-1
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发表时间：
1997-10
影响因子：
7.8
通讯作者：
Christopher T. Walsh;A. M. Gehring;P. Weinreb;Luis E. N. Quadri;R. Flugel
中科院分区：
文献类型：
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作者：
Christopher T. Walsh;A. M. Gehring;P. Weinreb;Luis E. N. Quadri;R. Flugel
在过去的一年里，随着磷脂酰基转移酶家族的鉴定，聚酮和非核糖体多肽生物合成的研究取得了重大进展，这是产生活性的、翻译后修饰的聚酮和多肽合成酶所必需的酶。脂肪酸、多肽和铁载体生物合成所需的磷脂酰基转移酶已经被表征，并记录了一个共同的序列，以便于将来更多催化磷脂酰基转移的蛋白质的鉴定。
The past year has witnessed a major advance in the study of polyketide and nonribosomal peptide biosynthesis with the identification of the phosphopantetheinyl transferase enzyme family, enzymes required to produce active, post-translationally modified polyketide and peptide synthases. Phosphopantetheinyl transferases required for fatty acid, peptide and siderophore biosynthesis have been characterized and a consensus sequence noted in order to facilitate future identification of additional proteins catalyzing phosphopantetheinyl transfer.