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Literature summary extracted from

  • Sakamoto, N.; Hatfield, G.W.; Moyed, H.S.
    Denaturation and renaturation of xanthosine 5¦-phosphate aminase (1972), J. Biol. Chem., 247, 5888-5891.
    View publication on PubMed

Organism

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

Renatured (Commentary)

EC Number Renatured (Comment) Organism
6.3.5.2 at low concentrations of the denaturants, up to 4.0 M urea and 1.2 M guanidine hydrochloride, inactivation is reversible. In 3.0-6.0 M guanidine hydrochloride the enzyme is extensively unfolded and partially, 15%, reassociable to the active form by removal of the denaturant. In 4.0 to 8.0 M urea and 1.2 to 3.0 M guanidine hydrochloride, the inactivation is irreversible due to the aggregation of the partially unfolded polypeptide chains Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.5.2 ATP + XMP + NH4+
-
 Escherichia coli AMP + diphosphate + GMP
-
 ?
6.3.5.2 ATP + XMP + NH4+
-
 Escherichia coli B96 AMP + diphosphate + GMP
-
 ?