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Mechanisms of cyanobactin biosynthesis

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CURRENT OPINION IN CHEMICAL BIOLOGY
卷 35, 期 -, 页码 80-88

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ELSEVIER SCI LTD
DOI: 10.1016/j.cbpa.2016.08.029

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资金

  1. European Research Council [339367]
  2. UK Biotechnology and Biological Sciences Research Council [K015508/1]
  3. Royal Society Wolfson Merit Award
  4. European Research Council (ERC) [339367] Funding Source: European Research Council (ERC)
  5. Biotechnology and Biological Sciences Research Council [BB/K015508/1] Funding Source: researchfish
  6. BBSRC [BB/K015508/1] Funding Source: UKRI

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Cyanobactins are a diverse collection of natural products that originate from short peptides made on a ribosome. The amino acids are modified in a series of transformations catalyzed by multiple enzymes. The patellamide pathway is the most well studied and characterized example. Here we review the structures and mechanisms of the enzymes that cleave peptide bonds, macrocyclise peptides, heterocyclise cysteine (as well as threonine and serine) residues, oxidize five-membered heterocycles and attach prenyl groups. Some enzymes operate by novel mechanisms which is of interest and in addition the enzymes uncouple recognition from catalysis. The normally tight relationship between these factors hinders biotechnology. The cyanobactin pathway may be particularly suitable for exploitation, with progress observed with in vivo and in vitro approaches.

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