Glyceraldehyde-3-phosphate dehydrogenase in the hyperthermophilic archaeon Sulfolobus solfataricus: Characterization and significance in glucose metabolism

A. Dello Russo, R. Rullo, M. Masullo, G. Ianniciello, P. Arcari, V. Bocchini

Research output: Contribution to journalArticle

Abstract

Glyceraldehyde-3-phosphate dehydrogenase in the archaeon Sulfolobus solfataricus (SsGAPD) has been purified 232 fold with an overall recovery of about 25%. The enzyme is a homomeric tetramer with an M(r) of 41 kDa/subunit. It utilizes either NAD+ or NADP+ as coenzyme but its affinity for the latter is about 50 fold higher. SsGAPD activity is maximum at 87°C. In the range 45-87°C the Arrhenius plot is linear and the activation energy is 55 kJ/mol. The enzyme is thermostable, with a half-life of 45 min at 87°C. The primary structure of SsGAPD shows 35% identity with that of other archaeal GAPDs. Its N-domain shows sequence motifs typical of the dinucleotide binding proteins while the catalytic C-terminal region contains a cysteine residue (C140), required for catalysis, that is conserved in all the archaeal, eukaryal and bacterial GAPDs. These remarks suggest that archaeal GAPDs show a convergent molecular evolution to the eukaryal and eubacterial enzymes in the catalytic region.

Original languageEnglish
Pages (from-to)123-135
Number of pages13
JournalBiochemistry and Molecular Biology International
Volume36
Issue number1
Publication statusPublished - 1995

ASJC Scopus subject areas

  • Biochemistry
  • Genetics
  • Molecular Biology

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