DMGDH
DMGDH (dimethylglycine dehydrogenase, also known as ME2GLYDH) is a mitochondrial flavoprotein oxidoreductase that catalyses the demethylation of N,N-dimethylglycine to sarcosine. It acts in the catabolism of choline and belongs to the GcvT family. Browse Assay Genie's current range of DMGDH research reagents below, or read on for the biology behind the target.
DMGDH catalyses the oxidative demethylation of N,N-dimethylglycine to form sarcosine, a step in the catabolism of choline. In vitro, the enzyme also shows activity with sarcosine. It is found as a monomer in the mitochondrial matrix and uses flavin adenine dinucleotide (FAD) and folate as cofactors, which is consistent with its place among the flavoproteins and oxidoreductases. It is a member of the GcvT family.
The DMGDH gene encodes the enzyme, and alternative splicing of the gene results in multiple transcript variants. The mature protein is annotated as dimethylglycine dehydrogenase, mitochondrial, and orthologues are present in mouse and rat, both named Dmgdh. Researchers studying the protein may use an DMGDH antibody or an DMGDH ELISA kit to investigate its levels in mitochondrial and metabolic contexts.
Mutation in the gene causes dimethylglycine dehydrogenase deficiency. This condition is characterised by a fishlike body odour, chronic muscle fatigue and elevated serum levels of the muscle form of creatine kinase. Because of this link, DMGDH is of interest in studies of choline metabolism, one-carbon and folate-dependent pathways, and inherited metabolic disorders.
DMGDH converts dimethylglycine to sarcosine, making it a key enzyme for studying how choline is broken down in the mitochondrial matrix.
Mutation in DMGDH causes dimethylglycine dehydrogenase deficiency, so the protein is relevant to research on this rare metabolic disorder.
The enzyme uses FAD and folate as cofactors, providing a model for studying flavin-dependent oxidoreductases of the GcvT family.
Deficiency is linked to chronic muscle fatigue and raised serum muscle creatine kinase, connecting DMGDH to studies of muscle metabolism.
DMGDH catalyses the oxidative demethylation of N,N-dimethylglycine to sarcosine in the mitochondrial matrix, as part of choline catabolism. It uses FAD and folate as cofactors and works as a monomer. In vitro it also shows activity with sarcosine.
DMGDH is the approved symbol for dimethylglycine dehydrogenase, and ME2GLYDH is an alias. UniProt lists the protein as dimethylglycine dehydrogenase, mitochondrial. Alternative splicing of the gene gives rise to multiple transcript variants, so check the datasheet of any product for its validated reactivity.
Mutation in DMGDH causes dimethylglycine dehydrogenase deficiency, with a fishlike body odour, chronic muscle fatigue and elevated serum muscle creatine kinase. Orthologues named Dmgdh exist in mouse and rat; check the datasheet of any product for its validated reactivity.
Other choline-pathway enzymes, mitochondrial flavoproteins and muscle markers relevant to DMGDH research.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q9UI17; product specifications from Assay Genie datasheets.