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Literature summary extracted from

  • Zalkin, H.
    GMP synthetase (1985), Methods Enzymol., 113, 273-278.
    View publication on PubMed

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.3.5.2 126000
-
 sedimentation equilibrium measurement Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
6.3.5.2 Escherichia coli
-
-
-
6.3.5.2 Escherichia coli B96
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.5.2
-
 Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.3.5.2 7.1
-
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.5.2 ATP + XMP + Gln it was previously reported that the activity responsible for GMP synthesis is strictly NH4+-dependent. It is possible that the glutamine-dependent activity is inactivated by Tris in the previously used 30-min end point assay Escherichia coli AMP + diphosphate + GMP + Glu
-
 ?
6.3.5.2 ATP + XMP + Gln maximal rate of the Gln-dependent activity is about 35% greater than that of NH4+-dependent activity Escherichia coli AMP + diphosphate + GMP + Glu
-
 ?
6.3.5.2 ATP + XMP + NH4+ it was previously reported that the activity responsible for GMP synthesis is strictly NH4+-dependent. It is possible that the glutamine-dependent activity is inactivated by Tris in the previously used 30-min end point assay Escherichia coli AMP + diphosphate + GMP
-
 ?
6.3.5.2 ATP + XMP + NH4+ maximal rate of the Gln-dependent activity is about 35% greater than that of NH4+-dependent activity Escherichia coli AMP + diphosphate + GMP
-
 ?
6.3.5.2 ATP + XMP + NH4+ it was previously reported that the activity responsible for GMP synthesis is strictly NH4+-dependent. It is possible that the glutamine-dependent activity is inactivated by Tris in the previously used 30-min end point assay Escherichia coli B96 AMP + diphosphate + GMP
-
 ?
6.3.5.2 ATP + XMP + NH4+ maximal rate of the Gln-dependent activity is about 35% greater than that of NH4+-dependent activity Escherichia coli B96 AMP + diphosphate + GMP
-
 ?
6.3.5.2 additional information maximal rate of glutaminase activity is 1.8fold greater than GMP synthetase activity Escherichia coli ?
-
 ?
6.3.5.2 additional information it was previously reported that the activity responsible for GMP synthesis is strictly NH4+-dependent. It is possible that the Gln-dependent activity is inactivated by Tris in the previously used 30-min end point assay Escherichia coli ?
-
 ?
6.3.5.2 additional information glutaminase activity Escherichia coli ?
-
 ?
6.3.5.2 additional information maximal rate of glutaminase activity is 1.8fold greater than GMP synthetase activity Escherichia coli B96 ?
-
 ?
6.3.5.2 additional information it was previously reported that the activity responsible for GMP synthesis is strictly NH4+-dependent. It is possible that the Gln-dependent activity is inactivated by Tris in the previously used 30-min end point assay Escherichia coli B96 ?
-
 ?
6.3.5.2 additional information glutaminase activity Escherichia coli B96 ?
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.5.2 8.3 8.5
-
 Escherichia coli