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ISSN 0582-9879 Acta Biochim et Biophysica Sinica 2004, 36(4):243-249 CN 31-1300/Q
Dissecting
and Exploiting Nonribosomal Peptide Synthetases
Qing-Tao SHEN, Xiu-Lan
CHEN, Cai-Yun SUN, and Yu-Zhong ZHANG*
( State Key Laboratory of Microbial Technology, Shandong University, Ji’nan
250100, China )
Abstract 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.
Key words nonribosomal peptide
synthetase; domain; combinatorial biosynthesis
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Received: December 19, 2003 Accepted:
February 5, 2004
This work was supported by the grants from the National High Technology Research
and Development Program of China (No. 2001AA246092) and the Science and Technology
Research and Development Program of Shandong Province (No. 030304)
*Corresponding author: Tel, 86-531-8364326; Fax, 86-531-8364326;E-mail, [email protected]