Stereoselectivity of fructose-1,6-bisphosphate aldolase in Thermus caldophilus

Jun Hyuck Lee, Jungdon Bae, Dooil Kim, Yongseok Choi, Young Jun Im, Sukhoon Koh, Joong Su Kim, Mun Kyoung Kim, Gil Bu Kang, Suk In Hong, Dae Sil Lee, Soo Hyun Eom

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

It was recently established that fructose-1,6-bisphosphate (FBP) aldolase (FBA) and tagatose-1,6-bisphosphate (TBP) aldolase (TBA), two class II aldolases, are highly specific for the diastereoselective synthesis of FBP and TBP from glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP), respectively. In this paper, we report on a FBA from the thermophile Thermus caldophilus GK24 (Tca) that produces both FBP and TBP from C3 substrates. Moreover, the FBP:TBP ratio could be adjusted by manipulating the concentrations of G3P and DHAP. This is the first native FBA known to show dual diastereoselectivity among the FBAs and TBAs characterized thus far. To explain the behavior of this enzyme, the X-ray crystal structure of the Tca FBA in complex with DHAP was determined at 2.2 Å resolution. It appears that as a result of alteration of five G3P binding residues, the substrate binding cavity of Tca FBA has a greater volume than those in the Escherichia coli FBA-phosphoglycolohydroxamate (PGH) and TBA-PGH complexes. We suggest that this steric difference underlies the difference in the diastereoselectivities of these class II aldolases.

Original languageEnglish
Pages (from-to)616-625
Number of pages10
JournalBiochemical and biophysical research communications
Volume347
Issue number3
DOIs
Publication statusPublished - 2006 Sep 1
Externally publishedYes

Keywords

  • Crystal structure
  • Fructose-1,6-bisphosphate aldolase
  • Stereoselectivity
  • Tagatose-1,6-bisphosphate aldolase

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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