Literature summary for 6.3.5.2 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.

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-
Escherichia coli B96	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
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

Renatured (Comment)

Organism

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)

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

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Release 2023.1 (January 2023)