Recombinant human GCDH (glutaryl-CoA dehydrogenase, mitochondrial)SKU: P-313

General description: 

Species: Homo sapiens

Source: Escherichia coli

Description: E.coli expressed, recombinant human glutaryl-CoA dehydrogenase (GCDH), mitochondrial. Produced with N-terminal 6xHis-tag and corresponds to amino acids: 45-438 of human GCDH (NP_000150.1).

Function:  GCDH 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 and utilizes electron transfer flavoprotein as its electron acceptor.


Formulation: intensely yellow liquid, containing 6xHis-tag human GCDH, stored in 20 mM Tris-HCl, pH 8.0, 10% glycerol, 1 µM FAD.

Purity: greater than 95% as determined by SDS-PAGE and Coomassie staining.

Concentration: greater than 5 mg/ml, as determined by BCA test.

Storage: Below minus 20°C. Minimize the number of freeze-thaw cycles.

Activity: Oxidation of glutaryl-CoA. Reduction of ETF (electron transfer flavoprotein)

References: Małecki, J., Ho, A. Y., Moen, A., Dahl, H. A., and Falnes, P. Ø. (2015) Human METTL20 is a mitochondrial lysine methyltransferase that targets the b subunit of electron transfer flavoprotein (ETFb) and modulates its activity. J. Biol. Chem. 290, 423–434.

About the scientist

Jedrzej Mieczyslaw Malecki

'Researcher in Pål Falnes group

About the Falnes group:
The Falnes group's main research interest is the identification of novel human enzymes involved regulation, such as the epigenetic modifications of DNA and chromatin proteins.
The cellular macromolecules DNA, RNA and protein are subject to numerous modifications, including methylations and hydroxylations. Such modifications often have regulatory roles, such as the epigenetic modifications of DNA and chromatin proteins. The major research interest in our group is the identification of novel human enzymes involved in the introduction and removal of such modifications, and to address the biological significance of the respective modifications. As such enzymes are often mutated or dysregulated in cancer, a better understanding of their function can possibly lead to improved cancer treatment or diagnosis. Recent work from the group have focused on methyltransferases and hydroxylases involved in modifying tRNA and protein, and demethylases removing deleterious methyl lesions from DNA. These studies typically involve both biochemical characterization of the modification enzymes, as well as analyses of the modifications and their roles in a cellular or organismal context.