Biosynthesis of trialkyl-substituted aromatic polyketide NFAT-133 involves unusual P450 monooxygenase-mediating aromatization and a putative metallo-beta-lactamase fold hydrolase

Biosynthesis of trialkyl-substituted aromatic polyketide NFAT-133 involves unusual P450 monooxygenase-mediating aromatization and a putative metallo-beta-lactamase fold hydrolase

The bacterial trialkyl-substituted aromatic polyketides are structurally featured with the unusual aromatic core in the middle of polyketide chain such as TM-123 (1), veramycin A (2), NFAT-133 (3) and benwamycin I (4), which were discovered from Streptomyces species and demonstrated with antidiabeti...

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Bibliographic Details
Main Authors: Ming Yang, Wanlu Li, Lin Zhou, Xiao Lin, Wenyu Zhang, Yaoyao Shen, Hai Deng, Hou-wen Lin, Yongjun Zhou
Format: Article
Language:English
Published: KeAi Communications Co., Ltd. 2023-09-01
Series:Synthetic and Systems Biotechnology
Subjects:
Thioesterase
Metallo hydrolase
Metallo-beta-lactamase
Aromatic polyketide
Polyketide synthase
P450 monooxygenase
Online Access:http://www.sciencedirect.com/science/article/pii/S2405805X23000339

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http://www.sciencedirect.com/science/article/pii/S2405805X23000339

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