BiOMaDe Technology Foundation, Nijenborgh 4, Groningen, The Netherlands.
Antonie Van Leeuwenhoek. 2010 May;97(4):319-33. doi: 10.1007/s10482-010-9418-4. Epub 2010 Feb 6.
This minireview focuses on the use of bacteria to introduce dehydroresidues and (methyl)lanthionines in (poly)peptides. It mainly describes the broad exploitation of bacteria containing lantibiotic enzymes for the engineering of these residues in a wide variety of peptides in particular in peptides unrelated to lantibiotics. Lantibiotic dehydratases dehydrate serines and threonines present in peptides preceded by a lantibiotic leader peptide thus forming dehydroalanine and dehydrobutyrine, respectively. These dehydroresidues can be coupled to cysteines thus forming (methyl)lanthionines. This coupling is catalysed by lantibiotic cyclases. The design, synthesis, and export of microbially engineered dehydroresidue and or lanthionine-containing peptides in non-lantibiotic peptides are reviewed, illustrated by some examples which demonstrate the high relevance of these special residues. This minireview is the first with special focus on the microbial engineering of nonlantibiotic peptides by exploiting lantibiotic enzymes.
这篇综述聚焦于利用细菌在（聚）肽中引入脱水残基和（甲基）硫醚键。主要描述了广泛利用含有类细菌素酶的细菌，在各种肽中，特别是与类细菌素无关的肽中，对这些残基进行工程改造。类细菌素脱水酶使位于类细菌素前导肽中的丝氨酸和苏氨酸脱水，分别形成脱水丙氨酸和脱水丁氨酸。这些脱水残基可以与半胱氨酸偶联，形成（甲基）硫醚键。这种偶联由类细菌素环化酶催化。本文综述了在非类细菌素肽中设计、合成和导出经过微生物工程改造的含有脱水残基和/或硫醚键的肽，并用一些实例说明了这些特殊残基的重要性。这是第一篇专门针对利用类细菌素酶对非类细菌素肽进行微生物工程改造的综述。
