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Literature summary for 6.3.1.21 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)

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

KM Value [mM]

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli P33221
-
-

Purification (Commentary)

Purification (Comment) Organism
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]

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

Substrates and Products (Substrate)

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

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

Synonyms

Synonyms Comment Organism
GAR transformylase
-
Escherichia coli
non-folate glycinamide ribonucleotide transformylase
-
Escherichia coli
PurT
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
37.6
-
formate recombinant enzyme, pH 8.0, 25°C Escherichia coli

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
Escherichia coli
additional information no activity with CTP, GTP, TTP, ITP, and aminoimidazolecarboxamide ribonucleotide triphosphate (ZTP) Escherichia coli

General Information

General Information Comment Organism
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
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