Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: KEGG:D02011 (
FAD
)
5,530
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The effect of riboflavin deficiency on the activity of L-gulonolactone oxidase [L-gulono-gamma-lactone: oxygen 2-oxidoreductase, EC 1.1.3.8] and on vitamin C status was studied. A marked decrease in the specific activity of L-gulonolactone oxidase was observed in the liver microsomes isolated from riboflavin-deficient rats: the specific activity was approx. one-third of that in the microsomes isolated from control rats. The L-ascorbic acid content in the liver of the riboflavin-deficient rats was approx. one-half of that in the liver of the control rats. It seems that the rate of production of L-ascorbic acid in the riboflavin-deficient rats is limited by the decreased level of L-gulonolactone oxidase activity. Immunotitration using rabbit antiserum directed to L-gulonolactone oxidase revealed that a substantial amount of an inactive form of this enzyme is present in the liver microsomes of the riboflavin-deficient rats.
L-Gulonolactone
oxidase activity in the microsomes of these rats increased by approx. 35% upon addition of
FAD
, but it was slightly decreased by the addition of FMN or riboflavin. These results indicate that the liver microsomes of the riboflavin-deficient rats contain a protein which exhibits L-gulonolactone oxidase activity upon addition of Fad.
...
PMID:L-gulonolactone oxidase activity and vitamin C status in riboflavin-deficient rats. 739 29
L-Gulono-gamma-lactone
oxidase, an enzyme functioning in L-ascorbic acid biosynthesis in higher animals, possesses a covalently-bound
FAD
as the prosthetic group. Catalytically-active enzyme was expressed in silkworm cells by a recombinant baculovirus encoding rat L-gulono-gamma-lactone oxidase. When recombinant enzyme was expressed under riboflavin-deficient conditions, most of it was found to be the apoprotein, as evidenced by an increase in enzymic activity upon addition of
FAD
to the assay mixture. Interestingly, the observed enzymic activity is thought to have been provoked by a noncovalent interaction between
FAD
and the apoprotein, since the covalent attachment of
FAD
was not demonstrated by a fluorometric gel-scanning experiment.
...
PMID:Production by a baculovirus expression system of the APO-protein of L-gulono-gamma-lactone oxidase, a flavoenzyme possessing a covalently-bound FAD. 795 Oct 49
