TY  - JOUR
AU  - Fauziah Ma’ruf, Ilma
AU  - Sasaki, Yuka
AU  - Kerbs, Anastasia
AU  - Nießer, Jochen
AU  - Sato, Yu
AU  - Taniguchi, Hironori
AU  - Okano, Kenji
AU  - Kitani, Shigeru
AU  - Restiawaty, Elvi
AU  - Akhmaloka
AU  - Honda, Kohsuke
TI  - Heterologous gene expression and characterization of two serine hydroxymethyltransferases from Thermoplasma acidophilum
JO  - Extremophiles
VL  - 25
IS  - 4
SN  - 1431-0651
CY  - Tokyo
PB  - Springer
M1  - FZJ-2021-06048
SP  - 393 - 402
PY  - 2021
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - 34196829
UR  - <Go to ISI:>//WOS:000668834700002
DO  - DOI:10.1007/s00792-021-01238-9
UR  - https://juser.fz-juelich.de/record/904478
ER  -