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Title 

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

Authors 

J H LeeJungdon BaeDooil KimY ChoiY J ImSukhoon KohJoong Su KimM K KimG B KangS I HongDae Sil LeeS H Eom

Publisher 

Elsevier

Issue Date 

2006

Citation 

Biochemical and Biophysical Research Communications, vol. 347, no. 3, pp. 616-625

Keywords 

crystal structurefructose-1,6-bisphosphate aldolasestereoselectivitytagatose-1,6-bisphosphate aldolasefructose bisphosphate aldolasetagatose 1,6 diphosphate aldolasethermus caldophilusfructose-bisphosphate aldolasefructosediphosphatesthermus

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 ? 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.

ISSN 

0006-291X

Link 

http://dx.doi.org/10.1016/j.bbrc.2006.06.139

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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