PXLP-K754-GLDC dimer decarboxylates Gly
Gly + Lipo-K107-GCSH + H+ → CO2 + AmMeLipoGCSH:SAMDLL
- Reactome
- R-HSA-5693967
- Compartment
- mitochondrial matrix
- Rhea
- RHEA:24305
Inputs
- GlyCHEBI:57305, C2H5NO2, mitochondrial matrix
- Lipo-K107-GCSHR-HSA-6793611, mitochondrial matrix
- H+CHEBI:15378, H, mitochondrial matrix
Outputs
- CO2CHEBI:16526, CO2, mitochondrial matrix
- AmMeLipoGCSH:SAMDLLR-HSA-5693969, mitochondrial matrix
Catalysed by
- glycine dehydrogenase (decarboxylating) activity of PXLP-K754-GLDC dimer [mitochondrial matrix]EC 1.4.4.2
Literature
- The glycine cleavage system. Molecular cloning of the chicken and human glycine decarboxylase cDNAs and some characteristics involved in the deduced protein structures J. Biol. Chem., 1991
- The primary structure of human H-protein of the glycine cleavage system deduced by cDNA cloning Biochem. Biophys. Res. Commun., 1991
- Lipoylation of H-protein of the glycine cleavage system. The effect of site-directed mutagenesis of amino acid residues around the lipoyllysine residue on the lipoate attachment FEBS Lett., 1991