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Literature summary for 6.3.5.2 extracted from

  • Lee, B.H.; Hartman, S.C.
    Preferential utilization of glutamine for amination of xanthosine 5'-phosphate to guanosine 5'-phosphate by purified enzymes from Escherichia coli (1974), Biochem. Biophys. Res. Commun., 60, 918-925.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
6-diazo-5-oxo-L-norleucine irreversible inhibition is dependent on presence of XMP, ATP and Mg2+ Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
60000
-
2 * 60000, SDS-PAGE in presence of 2-mercaptoethanol Escherichia coli
125000
-
gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli
-
B
-
Escherichia coli B / ATCC 11303
-
B
-
Escherichia coli B96
-
-
-

Purification (Commentary)

Purification (Comment) Organism
a single enzyme is responsible for Gln-dependent and NH4+-dependent reaction Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + XMP + Gln a single enzyme is responsible for Gln-dependent and NH4+ dependent reaction Escherichia coli AMP + diphosphate + GMP + Glu
-
?
ATP + XMP + Gln a single enzyme is responsible for Gln-dependent and NH4+ dependent reaction Escherichia coli B / ATCC 11303 AMP + diphosphate + GMP + Glu
-
?
ATP + XMP + Gln a single enzyme is responsible for Gln-dependent and NH4+ dependent reaction Escherichia coli B96 AMP + diphosphate + GMP + Glu
-
?
ATP + XMP + NH4+ a single enzyme is responsible for Gln-dependent and NH4+ dependent reaction Escherichia coli AMP + diphosphate + GMP
-
?
ATP + XMP + NH4+ a single enzyme is responsible for Gln-dependent and NH4+ dependent reaction Escherichia coli B / ATCC 11303 AMP + diphosphate + GMP
-
?
ATP + XMP + NH4+ a single enzyme is responsible for Gln-dependent and NH4+ dependent reaction Escherichia coli B96 AMP + diphosphate + GMP
-
?

Subunits

Subunits Comment Organism
dimer 2 * 60000, SDS-PAGE in presence of 2-mercaptoethanol Escherichia coli