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Literature summary extracted from

  • Holmes, E.W.
    Kinetic, physical, and regulatory properties of amidophosphoribosyltransferase (1981), Adv. Enzyme Regul., 19, 215-231.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.2.14 0.14 0.48 5-phospho-alpha-D-ribose 1-diphosphate
-
 Homo sapiens
2.4.2.14 0.47
-
 5-phospho-alpha-D-ribose 1-diphosphate adenocarcinoma 755 Homo sapiens
2.4.2.14 0.57
-
 5-phospho-alpha-D-ribose 1-diphosphate
-
 Mus musculus
2.4.2.14 1 4.5 L-glutamine
-
 Homo sapiens
2.4.2.14 1.24 1.5 L-glutamine
-
 Rattus norvegicus
2.4.2.14 1.8
-
 L-glutamine adenocarcinoma 755 Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.2.14 Fe
-
 Columba livia
2.4.2.14 Fe loss of activity after oxidation of the iron-sulfur center Mus musculus
2.4.2.14 Fe enzyme contains a [4Fe-4S] cluster Cricetulus griseus
2.4.2.14 Fe enzyme contains a [4Fe-4S] cluster Bacillus subtilis
2.4.2.14 Fe enzyme contains a [4Fe-4S] cluster Mus musculus
2.4.2.14 Fe enzyme contains a [4Fe-4S] cluster Homo sapiens
2.4.2.14 additional information
-
 Escherichia coli
2.4.2.14 additional information 4Fe-4S-cluster Cricetulus griseus
2.4.2.14 additional information 4Fe-4S-cluster Bacillus subtilis
2.4.2.14 additional information 4Fe-4S-cluster Mus musculus
2.4.2.14 additional information 4Fe-4S-cluster Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.2.14 additional information
-
 the smaller molecular weight form of the liver enzyme is observed when incubated with purine nucleotides, the smaller one when incubated with phosphoribosyldiphosphate Columba livia
2.4.2.14 additional information
-
 enzymes from human placenta, Chinese hamster fibroblasts and mouse liver exist in two molecular weight forms, the larger one is observed when incubated with purine nucleotides, the smaller one when incubated with phosphoribosyldiphosphate Cricetulus griseus
2.4.2.14 additional information
-
 enzymes from human placenta, Chinese hamster fibroblasts and mouse liver exist in two molecular weight forms, the larger one is observed when incubated with purine nucleotides, the smaller one when incubated with phosphoribosyldiphosphate Mus musculus
2.4.2.14 additional information
-
 enzymes from human placenta, Chinese hamster fibroblasts and mouse liver exist in two molecular weight forms, the larger one is observed when incubated with purine nucleotides, the smaller one when incubated with phosphoribosyldiphosphate Homo sapiens
2.4.2.14 127000
-
 liver small form Mus musculus
2.4.2.14 133000
-
 placenta small form, large form is converted to small form by incubation with phosphoribosyldiphosphate Homo sapiens
2.4.2.14 170000
-
 placenta large form, in the presence of AMP or GMP Homo sapiens
2.4.2.14 215000
-
 gel filtration Rattus norvegicus
2.4.2.14 215000
-
 only one enzyme form Rattus norvegicus
2.4.2.14 270000
-
 placenta, large form, small form is converted to large form by incubation with purine nucleotides, large form presumably catalytically inactive Homo sapiens
2.4.2.14 292000
-
 liver, large form Mus musculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.2.14 L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O Rattus norvegicus
-
 L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
 ?
2.4.2.14 L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O Cricetulus griseus first reaction in de-novo pathway of purine biosynthesis L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
 ?
2.4.2.14 L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O Bacillus subtilis first reaction in de-novo pathway of purine biosynthesis L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
 ?
2.4.2.14 L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O Mus musculus first reaction in de-novo pathway of purine biosynthesis L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
 ?
2.4.2.14 L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O Escherichia coli first reaction in de-novo pathway of purine biosynthesis L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
 ?
2.4.2.14 L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O Homo sapiens first reaction in de-novo pathway of purine biosynthesis L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
 ?
2.4.2.14 L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O Columba livia first reaction in de-novo pathway of purine biosynthesis L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.14 Bacillus subtilis
-
-
-
2.4.2.14 Columba livia
-
-
-
2.4.2.14 Cricetulus griseus
-
-
-
2.4.2.14 Escherichia coli
-
-
-
2.4.2.14 Homo sapiens
-
-
-
2.4.2.14 Mus musculus
-
-
-
2.4.2.14 Rattus norvegicus
-
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
2.4.2.14 amido- and aminotransferase activity is lost after exposure to oxygen Mus musculus
2.4.2.14 oxygen sensitive enzyme Cricetulus griseus
2.4.2.14 oxygen sensitive enzyme Mus musculus
2.4.2.14 oxygen sensitive enzyme Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.2.14 adenocarcinoma cell adenocarcinoma 755 Homo sapiens
-
2.4.2.14 erythroleukemia cell
-
 Mus musculus
-
2.4.2.14 fibroblast
-
 Cricetulus griseus
-
2.4.2.14 leukocyte
-
 Homo sapiens
-
2.4.2.14 liver
-
 Mus musculus
-
2.4.2.14 liver
-
 Rattus norvegicus
-
2.4.2.14 liver
-
 Columba livia
-
2.4.2.14 placenta
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.2.14 L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
-
 Cricetulus griseus 5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
 ?
2.4.2.14 L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
-
 Bacillus subtilis 5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
 ?
2.4.2.14 L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
-
 Mus musculus 5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
 ?
2.4.2.14 L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
-
 Escherichia coli 5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
 ?
2.4.2.14 L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
-
 Rattus norvegicus 5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
 ?
2.4.2.14 L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
-
 Columba livia 5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
 ?
2.4.2.14 L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O glutamine binding site distinct from NH3-site Homo sapiens 5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate
-
 ?
2.4.2.14 L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
-
 Rattus norvegicus L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
 ?
2.4.2.14 L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O first reaction in de-novo pathway of purine biosynthesis Cricetulus griseus L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
 ?
2.4.2.14 L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O first reaction in de-novo pathway of purine biosynthesis Bacillus subtilis L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
 ?
2.4.2.14 L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O first reaction in de-novo pathway of purine biosynthesis Mus musculus L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
 ?
2.4.2.14 L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O first reaction in de-novo pathway of purine biosynthesis Escherichia coli L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
 ?
2.4.2.14 L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O first reaction in de-novo pathway of purine biosynthesis Homo sapiens L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
 ?
2.4.2.14 L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O first reaction in de-novo pathway of purine biosynthesis Columba livia L-glutamate + 5-phospho-beta-D-ribosylamine + diphosphate
-
 ?
2.4.2.14 NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
-
 Cricetulus griseus 5-phospho-beta-D-ribosylamine + diphosphate
-
 ?
2.4.2.14 NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
-
 Bacillus subtilis 5-phospho-beta-D-ribosylamine + diphosphate
-
 ?
2.4.2.14 NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
-
 Mus musculus 5-phospho-beta-D-ribosylamine + diphosphate
-
 ?
2.4.2.14 NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
-
 Escherichia coli 5-phospho-beta-D-ribosylamine + diphosphate
-
 ?
2.4.2.14 NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O
-
 Columba livia 5-phospho-beta-D-ribosylamine + diphosphate
-
 ?
2.4.2.14 NH3 + 5-phospho-alpha-D-ribose 1-diphosphate + H2O NH3-binding site is distinct from glutamine-site Homo sapiens 5-phospho-beta-D-ribosylamine + diphosphate
-
 ?