An unusual metal-bound 4-fluorothreonine transaldolase from Streptomyces sp. MA37 catalyses promiscuous transaldol reactions
dc.contributor.author | Kyeremeh, K. | |
dc.contributor.author | Wu, L. | |
dc.contributor.author | Tong, M.H. | |
dc.contributor.author | Raab, A. | |
dc.contributor.author | Fang, Q. | |
dc.contributor.author | Wang, S. | |
dc.contributor.author | Yu, Y. | |
dc.contributor.author | Deng, H. | |
dc.date.accessioned | 2020-07-07T09:21:08Z | |
dc.date.available | 2020-07-07T09:21:08Z | |
dc.date.issued | 2020-03-06 | |
dc.description | Research Article | en_US |
dc.description.abstract | β-Hydroxy-α-amino acids (βH-AAs) are key components of many bioactive molecules as well as exist as specialised metabolites. Among these βH-AAs, 4-fluorothreonine (4-FT) is the only naturally occurring fluorinated AA discovered thus far. Here we report overexpression and biochemical characterisation of 4-fluorothreonine transaldolase from Streptomyces sp. MA37 (FTaseMA), a homologue of FTase previously identified in the biosynthesis of 4-FT in S. cattleya. FTaseMA displays considerable substrate plasticity to generate 4-FT as well as other β-hydroxy-α-amino acids with various functionalities at C4 position, giving the prospect of new chemo-enzymatic applications. The enzyme has a hybrid of two catalytic domains, serine hydroxymethyltransferase (S) and aldolase (A). Site-directed mutagenesis allowed the identification of the key residues of FTases, suggesting that the active site of A domain has a historical reminiscent feature in metal-dependent aldolases. Elemental analysis demonstrated that FTaseMA is indeed a Zn2+-dependent enzyme, the first example of pyridoxal phosphate (PLP) enzyme family fused with a metal-binding domain carrying out a distinct catalytic role. Finally, FTaseMA showed divergent evolutionary origin with other PLP dependent enzymes | en_US |
dc.description.sponsorship | IBioIC PhD studentship (LW), Leverhulme Trust Research Project (HD and MHT, project No. RPG-2014-418), The Elphinstone Scholarship of University of Aberdeen (QF), Leverhulme Trust-Royal Society Africa award (KK and HD, AA090088) and the jointly funded UK Medical Research Council – UK Department for International Development (MRC/DFID) Concordat agreement African Research Leaders Award (KK and HD, MR/S00520X/1), Biotechnology and Biological Sciences Research Council UK (HD and SW, BB/P00380X/1) and National Natural Science Foundation of China (31,570,033, 31,811,530,299, and 31,870,035 to YY), and the Royal Society-NSFC Newton Mobility Grant Award (IEC\NSFC\170,617 to HD and YY). | en_US |
dc.identifier.citation | Wu, L., Tong, M.H., Raab, A. et al. An unusual metal-bound 4-fluorothreonine transaldolase from Streptomyces sp. MA37 catalyses promiscuous transaldol reactions. Appl Microbiol Biotechnol 104, 3885–3896 (2020). https://doi.org/10.1007/s00253-020-10497-z | en_US |
dc.identifier.other | Applied Microbiology and Biotechnology | |
dc.identifier.uri | http://ugspace.ug.edu.gh/handle/123456789/35459 | |
dc.language.iso | en | en_US |
dc.publisher | Applied Microbiology and Biotechnology | en_US |
dc.relation.ispartofseries | 104;2020 | |
dc.subject | β-Hydroxy-α-amino acids | en_US |
dc.subject | 4-fluorothreonine | en_US |
dc.subject | 4-fluorothreonine transaldolase | en_US |
dc.subject | Transaldolation | en_US |
dc.subject | Streptomyces sp. | en_US |
dc.subject | MA37 | en_US |
dc.title | An unusual metal-bound 4-fluorothreonine transaldolase from Streptomyces sp. MA37 catalyses promiscuous transaldol reactions | en_US |
dc.type | Article | en_US |
Files
Original bundle
1 - 1 of 1
Loading...
- Name:
- An-unusual-metalbound-4fluorothreonine-transaldolase-from-Streptomyces-sp-MA37-catalyses-promiscuous-transaldol-reactionsApplied-Microbiology-and-Biotechnology.pdf
- Size:
- 631.25 KB
- Format:
- Adobe Portable Document Format
- Description:
License bundle
1 - 1 of 1
No Thumbnail Available
- Name:
- license.txt
- Size:
- 1.6 KB
- Format:
- Item-specific license agreed upon to submission
- Description: