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Literature summary extracted from

  • Nygaard, P.; Smith, J.
    Evidence for a novel glycinamide ribonucleotide transformylase in Escherichia coli (1993), J. Bacteriol., 175, 3591-3597 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
6.3.1.21 additional information isolation of mutants defective in GAR transformylase activity, generation of single and double null mutants of genes purT and purN, phenotypes, overview Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.1.21 Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.1.21 ATP + formate + N1-(5-phospho-beta-D-ribosyl)glycinamide Escherichia coli
-
 ADP + phosphate + N2-formyl-N1-(5-phospho-beta-D-ribosyl)glycinamide
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.1.21 Escherichia coli P33221
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.1.21 ATP + formate + N1-(5-phospho-beta-D-ribosyl)glycinamide
-
 Escherichia coli ADP + phosphate + N2-formyl-N1-(5-phospho-beta-D-ribosyl)glycinamide
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.3.1.21 GAR transformylase
-
 Escherichia coli
6.3.1.21 GAR transformylase T
-
 Escherichia coli
6.3.1.21 glycinamide ribonucleotide transformylase
-
 Escherichia coli
6.3.1.21 PurT
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.3.1.21 37
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.1.21 8
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.1.21 ATP
-
 Escherichia coli

Expression

EC Number Organism Comment Expression
6.3.1.21 Escherichia coli regulation of the level of GAR transformylase T is controlled by the PurR protein and hypoxanthine. The purT operator sequence for PurR binding is similar to that reported for several pur regulons, and the gene is a single gene operon additional information

General Information

EC Number General Information Comment Organism
6.3.1.21 malfunction mutants defective in synthesis of purN- and purT-encoded enzymes are isolated. Only strains defective in both genes require an exogenous purine source for growth. Determination of GAR transformylase T activity in vitro requires formate as the Cl donor. Growth of purN mutants is inhibited by glycine. Under these conditions GAR accumulates. Addition of purine compounds or formate prevents growth inhibition Escherichia coli
6.3.1.21 metabolism purN- and purT-encoded enzymes are required for synthesis of N2-formyl-N1-(5-phospho-beta-D-ribosyl)glycinamide, both enzymes may function to ensure normal purine biosynthesis. Regulation of the level of GAR transformylase T is controlled by the PurR protein and hypoxanthine. The GAR transformylase T-catalyzed reaction might provide a pathway by which formate is utilized or rescued as a C1 unit, and the activity of the two different GAR transformylases might be determined by the availability of the cofactors, formate and 10-formyl-THF Escherichia coli