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: EC:1.1.1.1 (
alcohol dehydrogenase
)
9,284
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Aldehyde reductase [EC 1.1.1.2] and aldose reductase [EC 1.1.1.21] are monomeric NADPH-dependent oxidoreductases having wide substrate specificities for carbonyl compounds. These enzymes are implicated in the development of diabetic complications by catalyzing the reduction of glucose to sorbitol.
Enzyme inhibition
as a direct pharmacokinetic approach to the prevention of diabetic complications resulting from the hyperglycemia of diabetes has not been effective because of nonspecificity of the inhibitors and some appreciable side effects. To understand the structural and evolutionary relationship of these enzymes, we cloned and sequenced cDNAs coding for aldose and aldehyde reductases from human liver and placental cDNA libraries. Human placental aldose reductase (open reading frame of 316 amino acids) has a 65% identity (identical plus conservative substitutions) to human liver and placental
aldehyde reductase
(open reading frame of 325 amino acids). The two sequences have significant identity to 2,5-diketogluconic acid reductase from corynebacterium, frog rho-crystallin, and bovine lung prostaglandin F synthase (reductase). Southern hybridization analysis of human genomic DNA indicates a multigene system for aldose reductase, suggesting the existence of additional proteins. Thus, the aldo-keto reductase superfamily of proteins may have a more significant and hitherto not fully appreciated role in general cellular metabolism.
...
PMID:The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. 249 33
A multispectroscopic exploration was employed to investigate the interaction between the metallo-enzyme
alcohol dehydrogenase
(
ADH
) from yeast with bioflavonoid quercetin (QTN). Here, we have characterized the complex formation between QTN and Zn
2+
in aqueous solution and then examined the effect of such complex formation on the enzymatic activity of a zinc(II)-dependent enzyme
alcohol dehydrogenase
from yeast. We have observed an inhibition of enzymatic activity of
ADH
in presence of QTN.
Enzyme inhibition
kinetic experiments revealed QTN as a non-competitive inhibitor of yeast
ADH
. Perturbation of Circular dichroic (CD) spectrum of
ADH
in presence of QTN is observed due to the structural changes of
ADH
on complexation with the above flavonoid. Our results indicate a conformational change of
ADH
due to removal of Zn
2+
present in the enzyme by QTN. This was further established by molecular modeling study which shows that the flavonoid binds to the Zn
2+
ion which maintains the tertiary structure of the metallo-enzyme. So, QTN abstracts only half of the Zn
2+
ions present in the enzyme i.e. one Zn
2+
ion per monomer. From the present study, the structural alteration and loss of enzymatic activity of
ADH
are attributed to the complex formation between QTN and Zn
2+
.
...
PMID:Inhibitory effects of the dietary flavonoid quercetin on the enzyme activity of zinc(II)-dependent yeast alcohol dehydrogenase: Spectroscopic and molecular docking studies. 2786 57
