Biochemical and genetic characterization of fungal proline hydroxylase in echinocandin biosynthesis-Reference-Cited by-同舟云学术

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Biochemical and genetic characterization of fungal proline hydroxylase in echinocandin biosynthesis

Published:2018-07-09 Issue:18 Volume:102 Page:7877-7890
ISSN:0175-7598
Container-title:Applied Microbiology and Biotechnology
language:en
Short-container-title:Appl Microbiol Biotechnol

Author:

Zhang Feng,Liu Hui,Zhang Tao,Pijning Tjaard,Yu Liyan,Zhang Weixin,Liu Weifeng,Meng Xiangfeng

Funder

Natural Science Foundation of Shandong Province (CN)

China Postdoctoral Science Foundation

The Fundamental Research Funds of Shandong University

State Key Laboratory of Microbial Technology Open Projects Fund

Publisher

Springer Science and Business Media LLC

Subject

Applied Microbiology and Biotechnology,General Medicine,Biotechnology

Link

http://link.springer.com/article/10.1007/s00253-018-9179-y/fulltext.html

Reference39 articles.

1. Balkovec JM, Hughes DL, Masurekar PS, Sable CA, Schwartz RE, Singh SB (2014) Discovery and development of first in class antifungal caspofungin (CANCIDAS (R))—a case study. Nat Prod Rep 31(1):15–34. https://doi.org/10.1039/c3np70070d

2. Bills G, Li Y, Chen L, Yue Q, Niu XM, An Z (2014) New insights into the echinocandins and other fungal non-ribosomal peptides and peptaibiotics. Nat Prod Rep 31(10):1348–1375. https://doi.org/10.1039/c4np00046c

3. Cacho RA, Jiang W, Chooi YH, Walsh CT, Tang Y (2012) Identification and characterization of the echinocandin B biosynthetic gene cluster from Emericella rugulosa NRRL 11440. J Am Chem Soc 134(40):16781–16790. https://doi.org/10.1021/ja307220z

4. Chen L, Yue Q, Zhang X, Xiang M, Wang C, Li S, Che Y, Ortiz-Lopez FJ, Bills GF, Liu X, An Z (2013) Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in the fungus Glarea lozoyensis. BMC genomics 14:339. https://doi.org/10.1186/1471-2164-14-339

5. Clifton IJ, Hsueh LC, Baldwin JE, Harlos K, Schofield CJ (2001) Structure of proline 3-hydroxylase—evolution of the family of 2-oxoglutarate dependent oxygenases. Eur J Biochem 268(24):6625–6636. https://doi.org/10.1046/j.0014-2956.2001.02617.x

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