JBC, Vol. 251, Issue 2, 329-333, Jan, 1976

Escherichia coli glyoxalate carboligase. Properties and reconstitution with 5-deazaFAD and 1,5-dihydrodeazaFADH2

T. H. Cromartie and C. T. Walsh

Glyoxalate carboligase (EC 4.1.1.47) has been purified to electrophoretic homogeneity from Escherichia coli. The enzyme was found to be a dimer of subunits of identical molecular weight of 68,000. Resolution of the holoenzyme into apoenzyme and FAD led to a dissociation of the dimer into monomers. The apoenzyme could be reconsitituted to full catalytic activity with FAD or the flavin coenzyme analogue 5-deazaFAD. Reconstitution of the apoenzyme with the reduced flavin analogue 1,5-dihydro-5-deazaFADH2 led to the recovery of 50% of enzymatic activity. The reconstitution of apoglyoxalate carboligase with all three coenzymes followed Michaelis-Menten kinetics with Km values of 0.25, 0.74, and 0.72 muM for FAD deazaFAD, and deazaFADH2, respectively.
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