Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: KEGG:D02011 (FAD)
 5,530 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The acetylenic substrate, D-2-amino-4-pentynoic acid (D-propargylglycine), was oxidatively deaminated by hog kidney D-amino acid oxidase[EC 1.4.3.3], with accompanying inactivation of the enzyme. The flavin which was extracted by hot methanol from the inactivated enzyme was identical with authentic FAD by thin-layer chromatography and circular dichroism. The excitation spectrum of emission at 520 nm of the released flavin was very similar to the absorption spectrum of oxidized FAD. The released flavin was reduced by potassium borohydride. The apoenzyme prepared after propargylglycine treatment did not show restored D-amino acid oxidase activity on adding exogenous FAD. The absorption spectrum of this inactivated apoenzyme showed absorption peaks at 279 and 317 nm, and a shoulder at about 290 nm. These results strongly indicate that the inactivation reaction is a dynamic affinity labeling with D-propargylglycine which produces irreversible inactivation of the enzyme by a covalent modification of an amino acid residue at the active site.
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PMID:Affinity labeling of D-amino acid oxidase with an acetylenic substrate. 0 Mar 79

The clinical and biochemical phenotype of glutaric acidaemia type II (GAII) has led to the suggestion that the defect in the disorder affects electron transfer from primary FAD-containing dehydrogenases into the respiratory chain. Two proteins are involved in this process, i.e. electron transfer flavoprotein (ETF) and ETF dehydrogenase, an iron--sulphur flavoprotein with a distinctive EPR signal. Reliable catalytic assays for these proteins are not available, but both proteins have been purified and antisera against them prepared in rabbits. SDS-PAG electrophoresis of liver mitochondrial membranes from a GAII infant with congenital anomalies, locating ETF dehydrogenase with specific antiserum, showed no cross-reactive material. EPR of the same membranes showed a marked decrease in the ETF dehydrogenase signal. These results suggest that the defect in GAII in some patients is indeed in electron transport, and specifically in ETF dehydrogenase.
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PMID:Glutaric acidaemia type II (multiple acyl-CoA dehydrogenation deficiency). 643 42