TAILIEUCHUNG - Báo cáo Y học: Kinetic study of sn-glycerol-1-phosphate dehydrogenase from the aerobic hyperthermophilic archaeon, Aeropyrum pernix K1

A gene having high sequence homology (45–49%) with the glycerol-1-phosphate dehydrogenase gene from Methanobacterium thermoautotrophicum was cloned from the aerobic hyperthermophilic archaeon Aeropyrum pernix K1 (JCM 9820). This gene expressed in Escherichia coli with the pET vector system consists of 1113 nucleotides with an ATG initiation codon and a TAG termination codon. The molecular mass of the purified enzyme was estimated to be 38 kDa by SDS/PAGE and kDa by gel column chromatography, indicating presence as a dimer | Eur. J. Biochem. 269 969-976 2002 FEBS 2002 Kinetic study of sn-glycerol-1-phosphate dehydrogenase from the aerobic hyperthermophilic archaeon Aeropyrum pernix K1 Jin-Suk Han1 Yoshitsugu Kosugi2 Hiroyasu Ishida2 and Kazuhiko Ishikawa1 1National Institute of Advanced Industrial Science and Technology Ikeda Osaka Japan 2National Institute of Advanced Industrial Science and Technology Tsukuba Ibaraki Japan A gene having high sequence homology 45-49 with the glycerol-1-phosphate dehydrogenase gene from Methano-bacterium thermoautotrophicum was cloned from the aerobic hyperthermophilic archaeon Aeropyrum pernix K1 JCM 9820 . This gene expressed in Escherichia coli with the pET vector system consists of 1113 nucleotides with an ATG initiation codon and a TAG termination codon. The molecular mass of the purified enzyme was estimated to be 38 kDa by SDS PAGE and kDa by gel column chromatography indicating presence as a dimer. The optimum reaction temperature of this enzyme was observed to be 94-96 C at near neutral pH. This enzyme was subjected to two-substrate kinetic analysis. The enzyme showed substrate specificity for NAD P H-dependent dihydroxyacetone phosphate reduction and NAD -dependent glycerol-1-phosphate Gro1P oxida tion. NADP -dependent Gro1P oxidation was not observed with this enzyme. For the production of Gro1P in A. pernix cells NADPH is the preferred coenzyme rather than NADH. Gro1P acted as a noncompetitive inhibitor against dihydroxyacetone phosphate and NAD P H. However NAD P acted as a competitive inhibitor against NAD P H and as a noncompetitive inhibitor against dihydroxyacetone phosphate. This kinetic data indicates that the catalytic reaction by glycerol-1-phosphate dehydrogenase from A. pernix follows a ordered bi-bi mechanism. Keywords Aeropyrum pernix archaea glycerol-1-phosphate dehydrogenase ordered bi-bi mechanism hyperthermophile. Archaea are a phylogenetically distinct group that diverged from eubacteria and eukaryotes at an early .

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