Dissecting and exploiting nonribosomal peptide synthetases.
A large number of therapeutically useful cyclic and linear peptides of bacteria or fungal origin are synthesized via a template-directed, nucleic-acid-independent nonribosomal mechanism. This process is carried out by mega-enzymes called nonribosomal peptide synthetases (NRPSs). NRPSs contain repeated coordinated groups of active sites called modules, and each module is composed of several domains with different catalytic activities. The familiarity to these domains lays base for the future genetic engineering of NRPSs to generate entirely "unnature" products. The details about NRPSs domain structures and the exploitation of NRPSs are described in this review.
Shen
Qing-Tao
QT
State Key Laboratory of Microbial Technology, Shandong University, Ji 'nan, China.
Chen
Xiu-Lan
XL
Sun
Cai-Yun
CY
Zhang
Yu-Zhong
YZ
D000595:Amino Acid Sequence; D001665:Binding Sites; D020650:Combinatorial Chemistry Techniques; D005544:Forecasting; D009097:Multienzyme Complexes; D010453:Peptide Synthases / Q000138:chemical synthesis* / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D015202:Protein Engineering; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
D009097:Multienzyme Complexes; D010453:Peptide Synthases