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Literature summary extracted from

  • Li, H.; Fast, W.; Benkovic, S.J.
    Structural and functional modularity of proteins in the de novo purine biosynthetic pathway (2009), Protein Sci., 18, 881-892.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
6.3.4.18 additional information generation of six recombinant hybrid proteins combining functional domains of PurK and PurT, glycinamide ribonucleotide formyltransferase, on the basis of structural and sequence alignments, overview. The mutant chimeras are functional and show activity with different substrates, overview Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.4.18 additional information
-
 additional information kinetics of recombinant mutant proteins, overview Escherichia coli
6.3.4.18 0.0068
-
 ATP pH 8.0, 25°C, chimeric mutant with PurK activity Escherichia coli
6.3.4.18 0.0103
-
 5-amino-1(5-phospho-D-ribosyl)imidazole pH 8.0, 25°C, chimeric mutant with PurK activity Escherichia coli
6.3.4.18 0.048
-
 ATP pH 8.0, 25°C, wild-type PurK Escherichia coli
6.3.4.18 0.066
-
 5-amino-1(5-phospho-D-ribosyl)imidazole pH 8.0, 25°C, wild-type PurK Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.4.18 Mg2+
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.4.18 ATP + 5-amino-1(5-phospho-D-ribosyl)imidazole + HCO3- Escherichia coli
-
 ADP + phosphate + 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.4.18 Escherichia coli
-
 strains, DH-5alpha and BL21(DE3), and purK- strain K-12 MG1655, gene purK
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.3.4.18 0.23
-
 wild-type PurK, ADP formation Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.4.18 ATP + 5-amino-1(5-phospho-D-ribosyl)imidazole + HCO3-
-
 Escherichia coli ADP + phosphate + 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
-
 ?
6.3.4.18 ATP + 5-amino-1(5-phospho-D-ribosyl)imidazole + HCO3- catalytic steps are the formation of an acyl phosphate intermediate upon ATP cleavage, followed by the nucleophilic attack on the carboxyl carbon of the intermediates by the amino nitrogen of the mononucleotides, formation of acyl phosphate intermediates Escherichia coli ADP + phosphate + 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
-
 ?
6.3.4.18 additional information comparison of active site organization and reaction mechanism to purT-encoded glycinamide ribonucleotide formyltransferase, overview Escherichia coli ?
-
 ?

Subunits

EC Number Subunits Comment Organism
6.3.4.18 More comparison of tertiary structure and active site organization to purT-encoded glycinamide ribonucleotide formyltransferase, PurK shows a three domain structure Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
6.3.4.18 More PurK is a member of the ATP-grasp protein superfamily Escherichia coli
6.3.4.18 N5-carboxylaminoimidazole ribonucleotide synthetase
-
 Escherichia coli
6.3.4.18 PurK
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.3.4.18 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
6.3.4.18 0.87
-
 ATP pH 8.0, 25°C, chimeric mutant with PurK activity Escherichia coli
6.3.4.18 5.9
-
 ATP pH 8.0, 25°C, wild-type PurK Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.4.18 8
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.4.18 ATP
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
6.3.4.18 metabolism the enzyme is involved in the de novo purine biosynthetic pathway Escherichia coli

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
6.3.4.18 84
-
 ATP pH 8.0, 25°C, chimeric mutant with PurK activity Escherichia coli
6.3.4.18 89
-
 ATP pH 8.0, 25°C, wild-type PurK Escherichia coli
6.3.4.18 120
-
 5-amino-1(5-phospho-D-ribosyl)imidazole pH 8.0, 25°C, wild-type PurK Escherichia coli
6.3.4.18 130
-
 5-amino-1(5-phospho-D-ribosyl)imidazole pH 8.0, 25°C, chimeric mutant with PurK activity Escherichia coli