The presence of elements of a dinucleotide fold in UDP-glucose 4-epimerase from saccharomyces fragilis

Samanta, Ajoy K. ; Bhaduri, Amar (1982) The presence of elements of a dinucleotide fold in UDP-glucose 4-epimerase from saccharomyces fragilis Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 707 (1). pp. 129-132. ISSN 0167-4838

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/016748...

Related URL: http://dx.doi.org/10.1016/0167-4838(82)90405-8

Abstract

UDPglucose 4-epimerase (EC 5.1.3.2) from Saccharomyces fragilis is a holoenzyme containing 1 mol NAD per mol dimeric protein. The enzyme can be dissociated with p-chloromercuribenzoate and can be reconstituted in the presence of 2-mercaptoethanol and exogenous NAD. Using Cibacron blue F3GA in this reconstituting system, competition between NAD and the dye for the pyridine nucleotide-binding site could be demonstrated. Inactive holoenzyme containing Cibacron blue can also be obtained under these conditions. These data suggest the possible presence of elements of a dinucleotide fold in this enzyme.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:UDPglucose 4-epimerase; Dinucleotide Fold; Reconstitution; Nucleotide-binding Site
ID Code:26443
Deposited On:06 Dec 2010 12:31
Last Modified:16 May 2011 10:24

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