Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.4.1.27 extracted from

  • Yadav, U.; Sundd, M.
    Backbone chemical shift assignments of the glycine cleavage complex H protein of Escherichia coli (2018), Biomol. NMR Assign., 12, 163-165 .
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Synonyms

Synonyms Comment Organism
glycine cleavage complex
-
Escherichia coli

Expression

Organism Comment Expression
Escherichia coli the activity of the glycine cleavage complex is repressed by purines down
Escherichia coli the activity of the glycine cleavage complex is induced in the presence of exogenous glycine up

General Information

General Information Comment Organism
metabolism the enzyme is one of the four components that form the glycine cleavage complex (GCS), essential for the synthesis of C1 (one-carbon units) for cell metabolism, by the oxidative cleavage of glycine. The glycine cleavage complex (GCS), in cooperation with GCA (serine hydroxymethyltransferase) regulates the endogenous levels of glycine and C1 units in the cell. This system comprises four loosely associated proteins, namely GcvP (a pyridoxal phosphate-containing protein), GcvH (a protein that carries aminomethyl intermediate), GcvT (protein required for tetrahydrofolate-dependent reaction) and GcvL (a lipoamide dehydrogenase). GcvP decarboxylates glycine and relocates the remaining methylamine moiety to the lipoyl group of GcvH Escherichia coli