3myp

Publication Abstract from PubMed

Staphylococcus aureus LacD, a Class I tagatose-1,6-bisphosphate (TBP) aldolase, shows broadened substrate specificity by catalyzing the cleavage of 1,6-bisphosphate derivatives of d-tagatose, d-fructose, d-sorbose, and d-psicose. LacD.1 and LacD.2 are two closely-related Class I TBP aldolases in Streptococcus pyogenes. Here we have determined the crystal structures of S. aureus LacD and S. pyogenes LacD.1. Monomers of both enzymes are folded into a (beta/alpha)(8) barrel and two monomers associate tightly to form a dimer in the crystals. The structures suggest that the residues E189 and S300 of rabbit muscle Class I fructose-1,6-bisphosphate (FBP) aldolase are important for substrate specificity. When we mutated the corresponding residues of S. aureus LacD, the mutants (L165E, L275S, and L165E/L275S) showed enhanced substrate specificity toward FBP. STRUCTURED SUMMARY: lacDbinds to lacD by X-ray crystallography(View interaction) lacD1binds to lacD1 by X-ray crystallography(View interaction).

Crystal structures of LacD from Staphylococcus aureus and LacD.1 from Streptococcus pyogenes: Insights into substrate specificity and virulence gene regulation.,Lee SJ, Kim HS, Kim do J, Yoon HJ, Kim KH, Yoon JY, Suh SW FEBS Lett. 2011 Jan 21;585(2):307-12. Epub 2010 Dec 28. PMID:21192932^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.