期刊
ACS CHEMICAL BIOLOGY
卷 13, 期 9, 页码 2387-2391出版社
AMER CHEMICAL SOC
DOI: 10.1021/acschembio.8b00364
关键词
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资金
- National Science Foundation of China [31425001, 21632007, 21661140002, 31600049]
- Postdoctoral Science Foundation of China [2016M590357]
Maremycins are a group of structurally diverse 2,5-diketopiperazine natural products featuring a rare amino acid building block, S-methyl-L-cysteine (Me-Cys). Three freestanding nonribosomal peptide synthetase (NRPS) proteins from the maremycins biosynthetic pathway were proposed for the formation of the 2,5-diketopiperazine scaffold: MarQ MarM, and MarJ. MarQ displays flexible adenylation activity toward Cys, Me-Cys, Ser, and (S)-2,3-diaminopropanoic acid (DAP) and transfers these substrates to MarJ, which is the discrete peptidyl carrier protein (PCP). MarQ could also activate several other amino acids. The embedded methyltransferase (MT) domain in MarQ specifically catalyzes the thiol methylation of MarJ-tethered Cys. The in vitro reconstitution of MarQ and MarJ further provides clear evidence for the reaction sequence of methylation step on Cys. Our study on MarJ/Q tridomain cassette gains valuable insights into maremycins structure diversity and will be exploited to incorporate Me-Cys into natural products by combinatorial biosynthesis.
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