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

Linrui Wu, Ming Him Tong, Andrea Raab, Qing Fang, Shan Wang, Kwaku Kyeremeh, Yi Yu, Hai Deng* (Corresponding Author)

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)
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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.


Original languageEnglish
Pages (from-to)3885-3896
Number of pages12
JournalApplied Microbiology and Biotechnology
Volume104
Early online date6 Mar 2020
DOIs
Publication statusPublished - 1 May 2020

Keywords

  • beta-Hydroxy-alpha-amino acids
  • 4-fluorothreonine
  • 4-fluorothreonine transaldolase
  • Transaldolation
  • Streptomyces sp

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