An unusual metal-bound 4-fluorothreonine transaldolase from Streptomyces sp. MA37 catalyses promiscuous transaldol reactions

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dc.contributor.authorKyeremeh, K.
dc.contributor.authorWu, L.
dc.contributor.authorTong, M.H.
dc.contributor.authorRaab, A.
dc.contributor.authorFang, Q.
dc.contributor.authorWang, S.
dc.contributor.authorYu, Y.
dc.contributor.authorDeng, H.
dc.date.accessioned2020-07-07T09:21:08Z
dc.date.available2020-07-07T09:21:08Z
dc.date.issued2020-03-06
dc.descriptionResearch Articleen_US
dc.description.abstractβ-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 enzymesen_US
dc.description.sponsorshipIBioIC 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.citationWu, 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-zen_US
dc.identifier.otherApplied Microbiology and Biotechnology
dc.identifier.urihttp://ugspace.ug.edu.gh/handle/123456789/35459
dc.language.isoenen_US
dc.publisherApplied Microbiology and Biotechnologyen_US
dc.relation.ispartofseries104;2020
dc.subjectβ-Hydroxy-α-amino acidsen_US
dc.subject4-fluorothreonineen_US
dc.subject4-fluorothreonine transaldolaseen_US
dc.subjectTransaldolationen_US
dc.subjectStreptomyces sp.en_US
dc.subjectMA37en_US
dc.titleAn unusual metal-bound 4-fluorothreonine transaldolase from Streptomyces sp. MA37 catalyses promiscuous transaldol reactionsen_US
dc.typeArticleen_US

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