Atlas of nonribosomal peptide and polyketide biosynthetic pathways reveals common occurrence of nonmodular enzymes

Hao Wang1, David P. Fewer1, Liisa Holm2, Leo Rouhiainen3, Kaarina Sivonen3
1Division of Microbiology and Biotechnology, Department of Food and Environmental Sciences and.
2Institute of Biotechnology and Department of Biosciences, Viikki Biocenter, University of Helsinki, FIN-00014, Helsinki, Finland.
3aDivision of Microbiology and Biotechnology, Department of Food and Environmental Sciences and

Tóm tắt

Significance This study demonstrates the widespread distribution of nonribosomal peptide synthetase and modular polyketide synthase biosynthetic pathways across the three domains of life, by cataloging a total of 3,339 gene clusters from 2,699 genomes. Our analysis suggests that noncanonical nonmodular biosynthetic enzymes are common in bacteria. Proteobacteria , Actinobacteria , Firmicutes , and Cyanobacteria in bacteria and Ascomycota in fungi contained higher number of these gene clusters and are likely to produce a wide variety of nonribosomal peptide and polyketide types of natural products. The data generated here provide a basis for the exploration of nonribosomal peptide and polyketide biosynthetic capacity and present a compelling wealth of new information for natural product discovery.

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10.1126/science.282.5386.63

10.1146/annurev.micro.58.030603.123615

10.1038/nrmicro1287

10.1016/j.copbio.2007.09.009

10.1021/ar7000414

10.1016/S1367-5931(03)00020-6

10.1021/cr0503097

10.1002/iub.1005

10.1016/S1074-5521(99)80083-0

10.1128/MMBR.66.2.223-249.2002

10.1128/IAI.71.4.1794-1803.2003

10.1021/cr960029e

10.1002/1439-7633(20020603)3:6<490::AID-CBIC490>3.0.CO;2-N

10.1039/c3ra42661k

10.1016/j.cbpa.2005.08.001

L Du, B Shen, Biosynthesis of hybrid peptide-polyketide natural products. Curr Opin Drug Discov Devel 4, 215–228 (2001).

10.1111/j.1574-6976.2006.00022.x

10.1039/b706416k

10.1039/b514050c

10.1186/1471-2164-14-611

10.1371/journal.pgen.1003496

10.1371/journal.pone.0008926

10.1126/science.1156407

10.1007/s10126-009-9197-y

10.1073/pnas.0537286100

10.1093/molbev/msi193

10.1099/mic.0.27141-0

10.1021/ja304941d

10.1021/bi011852u

10.1126/science.1094318

10.1007/3-540-27055-8_2

10.1039/b817075b

10.1016/j.jbiotec.2003.08.004

10.1371/journal.pone.0028231

10.1016/S1074-5521(00)80001-0

10.1006/mben.2000.0171

10.1126/science.1193637

10.1002/anie.201207456

10.1016/j.chembiol.2004.01.005

10.1021/ja0100827

10.1016/S0076-6879(09)04808-3

10.1093/nar/gkr466

10.1093/nar/gkh340

10.1093/oxfordjournals.molbev.a026334

10.1093/sysbio/syq010

10.1093/molbev/msr121