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The protein encoded by GCDH belongs to the acyl-CoA dehydrogenase family. Additionally we are shipping Glutaryl-CoA Dehydrogenase Antibodies (66) and Glutaryl-CoA Dehydrogenase Kits (2) and many more products for this protein.
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We report the allele frequencies for three known Glutaric aciduria type I low excretors GCDH variants (M405V, V400M and R227P) and note that both the M405V and V400M variants are significantly more common in the population of African ancestry compared to the general population
Our data underscore the impact of GCDH protein interactions mediated by amino acid residues on the surface of GCDH required for proper enzymatic activity
Mutations in GCDH gene observed in the present study indicate genetic heterogeneity in GCDH gene among South Indian population. No definite genotype-phenotype correlations were observed.
Point mutation of GCDH gene is associated with glutaric academia type I.
29 GCDH mutations were identified in 23 glutaric aciduria type 1 patients, including 11 novel mutations
Data indicate a homozygous c.1244-2A> C mutation of the glutaryl-CoA dehydrogenase (GCDH) gene in both patients.
These cells displayed decreased levels of GCDH tetramer.
Identification of GCDH gene mutations in four patients with glutaric academia type I.
A homozygous, disease-segregating mutation (p.Val400Met) was identified in the glutaryl-CoA dehydrogenase (GCDH) gene at chromosome 19p13.
physiological concentrations of flavin adenine dinucleotide resulted in a spectacular enhancement of the thermal stabilities of GCDH and prevented enzymatic activity loss
Quinolinic acid increased lactate release in both Gcdh (+/+) and Gcdh (-/-) mice and reduced the activities of complex IV and creatine kinase only in the striatum of Gcdh (-/-) mice.
Using an experimental model with a phenotype similar to that of GA-I in humans-the Gcdh(-/-) mice under high lysine diet (Gcdh(-/-) -Lys (show LYZ Proteins))-we provide evidence that a reduction in cortical inhibition of Gcdh(-/-) -Lys (show LYZ Proteins) mice, probably induced by GAD (show GAD1 Proteins) dysfunction, leads to hyperexcitability and increased slow oscillations associated with neurologic abnormalities in glutaric academia type I.
The data of this study indicate higher susceptibility of Gcdh(-/-) mice to excitotoxic damage.
GCDH-defective astrocytes actively contribute to produce and accumulate GA and 3HGA when Lys (show LYZ Proteins) catabolism is stressed
L-pipecolate is a major degradation product from L-lysine in murine brain generated by alpha-deamination of this amino acid in Gcdh-deficient mouse model for glutaric aciduria type I.
Data show that glutaryl-Coenzyme A dehydrogenase Gcdh(-/-) knockout mice display elevated levels of glutaric acid (GA) and 3-hydroxyglutaric acid (3-OHGA) but do not spontaneously develop striatal lesions.
These results provide evidence that glutamate (show GRIN1 Proteins) receptor and transporter expression is higher in Gcdh-/- mice.
bioenergetic impairment may play an important role in the pathomechanisms underlying neurodegenerative changes in glutaryl-CoA dehydrogenase deficiency
Data show that pathologic events in glutaryl-CoA dehydrogenase-deficient mice/glutaric acidemia type I begin in neurons while lysine accumulation in the immature brain allows increased glutaric acid production and age-dependent injury.
The protein encoded by this gene belongs to the acyl-CoA dehydrogenase family. It catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and CO(2) in the degradative pathway of L-lysine, L-hydroxylysine, and L-tryptophan metabolism. It uses electron transfer flavoprotein as its electron acceptor. The enzyme exists in the mitochondrial matrix as a homotetramer of 45-kD subunits. Mutations in this gene result in the metabolic disorder glutaric aciduria type 1, which is also known as glutaric acidemia type I. Alternative splicing of this gene results in multiple transcript variants. A related pseudogene has been identified on chromosome 12.
glutaryl-CoA dehydrogenase, mitochondrial
, glutaryl-Coenzyme A dehydrogenase