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Literature summary extracted from

  • Marolewski, A.; Smith, J.; Benkovic, S.
    Cloning and characterization of a new purine biosynthetic enzyme a non-folate glycinamide ribonucleotide transformylase from E. coli (1994), Biochemistry, 33, 2531-2537 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.1.21 gene purT, recombinant enzyme expression in Escherichia coli strain TX635 from plasmid pJS455 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.1.21 additional information
-
 additional information steady-state kinetics Escherichia coli
6.3.1.21 0.0101
-
 N1-(5-phospho-beta-D-ribosyl)glycinamide recombinant enzyme, pH 8.0, 25°C Escherichia coli
6.3.1.21 0.045
-
 ATP recombinant enzyme, pH 8.0, 25°C, with formate Escherichia coli
6.3.1.21 0.319
-
 formate recombinant enzyme, pH 8.0, 25°C Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.1.21 Co2+ can only partially substitute for Mg2+, moderate to low activity Escherichia coli
6.3.1.21 Mg2+ required Escherichia coli
6.3.1.21 Mn2+ can only partially substitute for Mg2+, low activity 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
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.1.21 recombinant enzyme from Escherichia coli strain TX635 by streptomycin sulfate precipitation, dialysis, anion exchange chromatography, and ultrafiltration, followed by another different step of anion exchange chromatography, dialysis, and ultrafiltration Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.3.1.21 2.6
-
 purified recombinant enzyme, pH 8.0, 25°C, with Mn2+ Escherichia coli
6.3.1.21 17.3
-
 purified recombinant enzyme, pH 8.0, 25°C, with Co2+ Escherichia coli
6.3.1.21 52
-
 purified recombinant enzyme, pH 8.0, 25°C, with Mg2+ Escherichia coli

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
-
 ?
6.3.1.21 additional information radioactive assay monitoring the conversion of [14C]formate to fGAR or [alpha-32P] ATP to ADP. No activity with 10-formyl-5,8-dideazatetrahydrofolate (10-formyl-DDF), 5-formyl-THF, formyl-aminoimidazolecarboxamide ribonucleotide (fAICAR), formylmethionine, and formiminoglutamate as formyl donor. The enzyme shows a side reaction with ATP and acetate: cleavage of ATP in the presence of acetate to generate acetyl phosphate and ADP. The NMR study demonstrates that the purT GAR transformylase reaction proceeds through a transfer of atomic oxygen from formate to the 7-phosphoryl moiety of ATP. One interpretation is the intermediacy of formyl phosphate whose presence is also supported by the identification of acetyl phosphate as a product in the side reaction Escherichia coli ?
-
-

Subunits

EC Number Subunits Comment Organism
6.3.1.21 ? x * 42000, SDS-PAGE Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
6.3.1.21 GAR transformylase
-
 Escherichia coli
6.3.1.21 non-folate 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 25
-
 assay at Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.3.1.21 37.6
-
 formate recombinant enzyme, pH 8.0, 25°C 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
6.3.1.21 additional information no activity with CTP, GTP, TTP, ITP, and aminoimidazolecarboxamide ribonucleotide triphosphate (ZTP) Escherichia coli

General Information

EC Number General Information Comment Organism
6.3.1.21 metabolism PurT glycinamide ribonucleotide (GAR) transformylase is an alternative to the formyl-folate utilizing purN GAR transformylase. No significant homology exists between the two transformylases. But the PurT protein shows significant homology to the PurK protein, also involved in purine biosynthesis Escherichia coli
6.3.1.21 physiological function PurT glycinamide ribonucleotide (GAR) transformylase is an alternative to the formyl-folate utilizing purN GAR transformylase. Biologically relevant transformation of beta-GAR into fGAR Escherichia coli