2-Keto-3-deoxy-6-phosphogluconate KDPG aldolase

The carbon-carbon forming ability of aldolases has been limited in part by their narrow substrate utilization. Site-directed mutagenesis of various enzymes to alter their specificity has most often not produced the desired effect. Directed evolution approaches have furnished novel activities through multiple mutations of residues involved in recognition in no instance has a key catalytic residue been altered while activity is retained. Random mutagenesis resulted in a double mutant of E. coli 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase with reduced but measurable enzyme activity and a synthetically useful substrate profile (Wymer, 2001). 

Unlike other pyruvate aldolases, 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase (EC 4.1.2.14), which catalyzes the reversible condensation... 

Some initial studies have been made on KDPG aldolase (EC 4.1.2.14) which in vivo catalyzes the reversible condensation of the pyruvate with glyceraldehyde 3-phosphate (25) to form 2-keto-3-deoxy-6-phosphogluconate (KDPG - 26) (Scheme 9). The enzyme was found to accept a number of unnatural aldehydes as electrophiles. It was applied for the synthesis of KDG from glyceraldehyde [66]. 

Keto-3-deoxy-6-phosphogluconate aldolase (KDPG aldolase) 165... 

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