PMID:1107332
| Citation |
Cromartie, TH and Walsh, CT (1976) Escherichia coli glyoxalate carboligase. Properties and reconstitution with 5-deazaFAD and 1,5-dihydrodeazaFADH2. J. Biol. Chem. 251:329-33 |
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| Abstract |
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. |
| Links | |
| Keywords |
Binding Sites; Carboxy-Lyases/isolation & purification; Carboxy-Lyases/metabolism; Escherichia coli/enzymology; Flavin-Adenine Dinucleotide/analogs & derivatives; Flavin-Adenine Dinucleotide/pharmacology; Kinetics; Macromolecular Substances; Molecular Weight; Protein Binding; Spectrophotometry; Spectrophotometry, Ultraviolet |
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