Literature summary for 5.1.3.2 extracted from

Barat, B.; Bhattacharyya, D.
UDP-galactose 4-epimerase from Escherichia coli: formation of catalytic site during reversible folding (2001), Arch. Biochem. Biophys., 391, 188-196.

Search for more literature for 5.1.3.2

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
39000	-	2 * 39000	Escherichia coli

Organic Solvent Stability

Organic Solvent	Comment	Organism
urea	denaturation by 8 M urea at pH 7.0 causes 85% loss of ist secondary structure and dissociation of its constituent molecules	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
dilution of the denaturant urea by buffer at pH 8.5 leads to functional reconstitution of the dimeric holoenzyme. The refolding process is biphasic: after 2 min an equilibrium conformer is formed having 72% of its native secondary structure and by 60 min reactivation becomes complete. The early intermediate has lower energy of activation against thermal denaturation than the reactivated state	Escherichia coli

Subunits

Subunits	Comment	Organism
dimer	2 * 39000	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	covalently bound	Escherichia coli

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)