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@ARTICLE{FauziahMaruf:904478,
      author       = {Fauziah Ma’ruf, Ilma and Sasaki, Yuka and Kerbs,
                      Anastasia and Nießer, Jochen and Sato, Yu and Taniguchi,
                      Hironori and Okano, Kenji and Kitani, Shigeru and
                      Restiawaty, Elvi and Akhmaloka and Honda, Kohsuke},
      title        = {{H}eterologous gene expression and characterization of two
                      serine hydroxymethyltransferases from {T}hermoplasma
                      acidophilum},
      journal      = {Extremophiles},
      volume       = {25},
      number       = {4},
      issn         = {1431-0651},
      address      = {Tokyo},
      publisher    = {Springer},
      reportid     = {FZJ-2021-06048},
      pages        = {393 - 402},
      year         = {2021},
      abstract     = {Serine hydroxymethyltransferase (SHMT) and threonine
                      aldolase are classified as fold type I
                      pyridoxal-5’-phosphate-dependent enzymes and engaged in
                      glycine biosynthesis from serine and threonine,
                      respectively. The acidothermophilic archaeon Thermoplasma
                      acidophilum possesses two distinct SHMT genes, while there
                      is no gene encoding threonine aldolase in its genome. In the
                      present study, the two SHMT genes (Ta0811 and Ta1509) were
                      heterologously expressed in Escherichia coli and
                      Thermococcus kodakarensis, respectively, and biochemical
                      properties of their products were investigated. Ta1509
                      protein exhibited dual activities to catalyze
                      tetrahydrofolate (THF)-dependent serine cleavage and
                      THF-independent threonine cleavage, similar to other SHMTs
                      reported to date. In contrast, the Ta0811 protein lacks
                      amino acid residues involved in the THF-binding motif and
                      catalyzes only the THF-independent cleavage of threonine.
                      Kinetic analysis revealed that the threonine-cleavage
                      activity of the Ta0811 protein was 3.5 times higher than the
                      serine-cleavage activity of Ta1509 protein. In addition,
                      mRNA expression of Ta0811 gene in T. acidophilum was
                      approximately 20 times more abundant than that of Ta1509.
                      These observations suggest that retroaldol cleavage of
                      threonine, mediated by the Ta0811 protein, has a major role
                      in glycine biosynthesis in T. acidophilum.},
      cin          = {IBG-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBG-1-20101118},
      pnm          = {2172 - Utilization of renewable carbon and energy sources
                      and engineering of ecosystem functions (POF4-217)},
      pid          = {G:(DE-HGF)POF4-2172},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {34196829},
      UT           = {WOS:000668834700002},
      doi          = {10.1007/s00792-021-01238-9},
      url          = {https://juser.fz-juelich.de/record/904478},
}