Udpglucose 4-epimerase - Open Access .click

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Carbohydrate utilization in Streptococcus thermophilus: characterization of the genes for aldose 1-epimerase (mutarotase) and UDPglucose 4-epimerase [PDF]

Journal of Bacteriology, 1990
The complete nucleotide sequences of the genes encoding aldose 1-epimerase (mutarotase) (galM) and UDPglucose 4-epimerase (galE) and flanking regions of Streptococcus thermophilus have been determined. Both genes are located immediately upstream of the S. thermophilus lac operon.
Bert Poolman
exaly +14 more sources

UDPGlucose 4-epimerase from Saccharomyces fragilis. Allosteric kinetics with UDP-glucose as substrate [PDF]

Journal of Biological Chemistry, 1975
UDPglucose 4-epimerase from Saccharomyces fragilis catalyzes a freely reversible reaction between UDP-galactose and UDP-glucose. With UDP-galactose as the substrate the enzyme shows a classical hyperbolic kinetics but when UDP-glucose is used as the substrate a distinct allostericity is observed.
A Bhaduri
exaly +6 more sources

Distinct functional roles of two active site thiols in UDPglucose 4-epimerase from Kluyveromyces fragilis. [PDF]

Journal of Biological Chemistry, 1992
UDPglucose 4-epimerase from Kluyveromyces fragilis was earlier shown to have two conformationally vicinal thiols at the active site. Upon treatment with diamide, these thiols form a disulfide linkage across the subunits that results in coordinated loss of catalytic activity and coenzyme fluorescence (Ray, M., and Bhaduri, A. (1980) J. Biol. Chem.
A Bhaduri
exaly +6 more sources

An essential histidine residue for the activity of UDPglucose 4-epimerase from Kluyveromyces fragilis.

Journal of Biological Chemistry, 1992
UDPglucose 4-epimerase from Kluyveromyces fragilis was completely inactivated by diethylpyrocarbonate following pseudo-first order reaction kinetics. The pH profile of diethylpyrocarbonate inhibition and reversal of inhibition by hydroxylamine suggested specific modification of histidyl residues. Statistical analysis of the residual enzyme activity and
A Bhaduri
exaly +5 more sources

Microenvironment at the substrate binding subsite of the active site of UDPglucose 4-epimerase from Kluyveromyces fragilis using a fluorescent analog of UMP.

Indian journal of biochemistry & biophysics, 1992
A chromophorics and fluorescent analog of uridine 5'-monophosphate (UMP), a known competitive inhibitor of UDPglucose 4-epimerase was synthesised. This analog, namely 2',3'-O-(2,4,6-trinitrocyclohexadienylidene) uridine 5'-monophosphate, was found to be a powerful reversible inhibitor of UDPglucose 4-epimerase indicating its interaction with the ...
S, Ray, E, Ali, A, Bhaduri
openaire +1 more source

Molecular characterisation of Entamoeba histolytica UDP-glucose 4-epimerase, an enzyme able to provide building blocks for cyst wall formation. [PDF]