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   <subfield code="a">Biochemical characterization of glyceraldehyde-3-phosphate dehydrogenase from Thermococcus kodakarensis KOD1</subfield>
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   <subfield code="c">[Baolei Jia, Le Linh, Sangmin Lee, Bang Pham, Jinliang Liu, Hongyu Pan, Shihong Zhang, Gang-Won Cheong]</subfield>
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   <subfield code="a">Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an essential role in glycolysis by catalyzing the conversion of d-glyceraldehyde 3-phosphate (d-G3P) to 1,3-diphosphoglycerate using NAD+ as a cofactor. In this report, the GAPDH gene from the hyperthermophilic archaeon Thermococcus kodakarensis KOD1 (GAPDH-tk) was cloned and the protein was purified to homogeneity. GAPDH-tk exists as a homotetramer with a native molecular mass of 145kDa; the subunit molecular mass was 37kDa. GAPDH-tk is a thermostable protein with a half-life of 5h at 80-90°C. The apparent K m values for NAD+ and d-G3P were 77.8±7.5μM and 49.3±3.0μM, respectively, with V max values of 45.1±0.8U/mg and 59.6±1.3U/mg, respectively. Transmission electron microscopy (TEM) and image processing confirmed that GAPDH-tk has a tetrameric structure. Interestingly, GAPDH-tk migrates as high molecular mass forms (~232kDa and ~669kDa) in response to oxidative stress.</subfield>
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