Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus: Kinetic and structural properties

Marco Alvarez, Johan Ph Zeelen, Véronique Mainfroid, Françoise Rentier-Delrue, Joseph A. Martial, Lode Wyns, Rik K. Wierenga, Dominique Maes

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127 Citations (Scopus)

Abstract

The purification and characterization of triose-phosphate isomerase from the psychrophilic bacterium Vibrio marinus (vTIM) is described. Crystal structures of the vTIM-sulfate complex and the vTIM-2-phosphoglycolate complex (at a 2.7-Å resolution) are also presented. The optimal growth temperature of Vibrio marinus is 15 °C. Stability studies show that vTIM is an unstable protein with a half-life of only 10 min at 25 °C. The vTIM sequence is most closely related to the sequence of Escherichia coli TIM (eTIM) (66% identity), and several unique structural features described for eTIM are also seen in vTIM, but eTIM is considerably more stable. The T(d) values of vTIM and eIM determined by calorimetric studies, are 41 and 54 °C, respectively. Amino acid sequence comparison reveals that vTIM has an alanine in loop 8 (at position 238), whereas all other TIM sequences known to date have a serine. The vTIM mutant A238S was produced and characterized. Compared with wild type, the catalytic efficiency of the A238S mutant is somewhat reduced, and its stability is considerably increased.

Original languageEnglish
Pages (from-to)2199-2206
Number of pages8
JournalJournal of Biological Chemistry
Volume273
Issue number4
DOIs
Publication statusPublished - 23 Jan 1998

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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