Revealing substrate promiscuity of 1-deoxy-D-xylulose 5-phosphate synthase.
A study of DXP synthase has revealed flexibility in the acceptor substrate binding pocket for nonpolar substrates and has uncovered new details of the catalytic mechanism to show that pyruvate can act as both donor and acceptor substrate.
Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
Leighanne A
LA
Brammer
Caren Freel
CF
Meyers
D000447:Aldehydes / Q000378:metabolism; D055162:Biocatalysis; D002851:Chromatography, High Pressure Liquid; D004926:Escherichia coli / Q000201:enzymology; D011773:Pyruvates / Q000378:metabolism; D013379:Substrate Specificity; D014166:Transferases / Q000378:metabolism*
D000447:Aldehydes; D011773:Pyruvates; D014166:Transferases; C109461:deoxyxylulose-5-phosphate synthase