期刊
JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY
卷 48, 期 3-4, 页码 -出版社
OXFORD UNIV PRESS
DOI: 10.1093/jimb/kuab023
关键词
Cyclopeptide; Biocatalyst; Cyclase
资金
- Asahi Glass Foundation
- Naito Foundation
- Uehara Memorial Foundation
- Sumitomo Foundation-Grant for Basic Science Research Projects
- Daiichi Sankyo Foundation of Life Science
- Japan Agency for Medical Research and Development (AMED) [JP19ae0101045]
- Japan Science and Technology Agency (JST) [JPMJAX201F, JPMJTR20US]
- Ministry of Education, Culture, Sports, Science and Technology (MEXT), Japan (JSPS KAKENHI) [JP16703511, JP18056499, JP19178402]
PenA, a PBP-type thioesterases, is specialized in small peptide cyclization, which is suggested to be determined by a computational model providing a possible structural rationale for its altered specificity for substrate chain lengths.
Penicillin-binding protein-type thioesterases (PBP-type TEs) are a recently identified group of peptide cyclases that catalyze head-to-tail macrolactamization of nonribosomal peptides. PenA, a new member of this group, is involved in the biosyntheses of cyclic pentapeptides. In this study, we demonstrated the enzymatic activity of PenA in vitro, and analyzed its substrate scope with a series of synthetic substrates. A comparison of the reaction profiles between PenA and SurE, a representative PBP-type TE, showed that PenA is more specialized for small peptide cyclization. A computational model provided a possible structural rationale for the altered specificity for substrate chain lengths.
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