Glycine dehydrogenase (decarboxylating)

Glycine dehydrogenase (decarboxylating)
Identifiers
Symbols GLDC; GCE; GCSP; HYGN1; MGC138198; MGC138200
External IDs OMIM: 238300 MGI: 1341155 HomoloGene: 141 GeneCards: GLDC Gene
EC number 1.4.4.2
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 2731 104174
Ensembl ENSG00000178445 ENSMUSG00000024827
UniProt P23378 Q9CRJ4
RefSeq (mRNA) NM_000170 NM_138595.1
RefSeq (protein) NP_000161 NP_613061.1
Location (UCSC) Chr 9:
6.53 – 6.65 Mb		 Chr 19:
30.17 – 30.25 Mb
PubMed search [1] [2]
glycine dehydrogenase (decarboxylating)
Identifiers
EC number 1.4.4.2
CAS number 37259-67-9
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

Glycine dehydrogenase [decarboxylating], mitochondrial also known as glycine cleavage system P protein or glycine decarboxylase is an enzyme that in humans is encoded by the GLDC gene.[1][2][3]

Contents

Reaction

Glycine dehydrogenase (decarboxylating) (EC 1.4.4.2) is an enzyme that catalyzes the following chemical reaction:

glycine + H-protein-lipoyllysine \rightleftharpoons H-protein-S-aminomethyldihydrolipoyllysine + CO2

Thus, the two substrates of this enzyme are glycine and H-protein-lipoyllysine, whereas its two products are H-protein-S-aminomethyldihydrolipoyllysine and CO2.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with a disulfide as acceptor. This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate.

Function

Glycine decarboxylase is a P-protein of the glycine cleavage system in eukaryotes. The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor. Carbon dioxide is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.

Degradation of glycine is brought about by the glycine cleavage system, which is composed of four mitochondrial protein components: P protein (a pyridoxal phosphate-dependent glycine decarboxylase), H protein (a lipoic acid-containing protein), T protein (a tetrahydrofolate-requiring enzyme), and L protein (a lipoamide dehydrogenase).[3]

Clinical significance

Glycine encephalopathy may be due to a defect in any one of these enzymes.[3]

References

  1. ^ Kume A, Koyata H, Sakakibara T, Ishiguro Y, Kure S, Hiraga K (Mar 1991). "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 266 (5): 3323–9. PMID 1993704. 
  2. ^ Kure S, Narisawa K, Tada K (Mar 1991). "Structural and expression analyses of normal and mutant mRNA encoding glycine decarboxylase: three-base deletion in mRNA causes nonketotic hyperglycinemia". Biochem Biophys Res Commun 174 (3): 1176–82. doi:10.1016/0006-291X(91)91545-N. PMID 1996985. 
  3. ^ a b c "Entrez Gene: GLDC glycine dehydrogenase (decarboxylating)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2731. 

Further reading

}}