Escherichia coli uridine diphosphate galactose 4-epimerase: circular dichroism of the protein and protein bound dihydronicotinamide adenine dinucleotide

Biochemistry ◽  
1978 ◽  
Vol 17 (3) ◽  
pp. 516-520 ◽  
Author(s):  
Shan S. Wong ◽  
Joseph Y. Cassim ◽  
Perry A. Frey
Keyword(s):  
Escherichia Coli ◽  
Circular Dichroism ◽  
Uridine Diphosphate ◽  
Circular Dichroïsm ◽  
Uridine Diphosphate Galactose

scholarly journals Circular dichroism investigation of Escherichia coli adenylate kinase.

1987 ◽  
Vol 262 (6) ◽  
pp. 2502-2506
Author(s):  
M. Monnot ◽  
A.M. Gilles ◽  
I.S. Girons ◽  
S. Michelson ◽  
O. Bârzu ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Circular Dichroism ◽  
Adenylate Kinase ◽  
Circular Dichroïsm

Folding Pathway of Escherichia coli Ribonuclease HI: A Circular Dichroism, Fluorescence, and NMR Study

Biochemistry ◽  
1995 ◽  
Vol 34 (51) ◽  
pp. 16552-16562 ◽  
Author(s):  
Kazuhiko Yamasaki ◽  
Kyoko Ogasahara ◽  
Katsuhide Yutani ◽  
Motohisa Oobatake ◽  
Shigenori Kanaya
Keyword(s):  
Escherichia Coli ◽  
Circular Dichroism ◽  
Folding Pathway ◽  
Nmr Study ◽  
Circular Dichroïsm

Physical studies on the ribosomal "A" protein from two archaebacteria, Halobacterium cutirubrum and Methanobacterium thermoautotrophicum

1984 ◽  
Vol 62 (1) ◽  
pp. 44-48 ◽  
Author(s):  
A. T. Gudkov ◽  
S. Yu Venyaminov ◽  
A. T. Matheson
Keyword(s):  
Escherichia Coli ◽  
Circular Dichroism ◽  
Secondary Structure ◽  
Quaternary Structure ◽  
Methanobacterium Thermoautotrophicum ◽  
Sedimentation Equilibrium ◽  
Effect Of Temperature ◽  
Extreme Halophile ◽  
Moderate Halophile ◽  
Circular Dichroïsm

Physical studies on the effect of temperature and ionic conditions on the secondary, tertiary, and quaternary structure of the ribosomal "A" protein, equivalent to L7/L12 in Escherichia coli, from two archaebacteria were performed using circular dichroism and sedimentation equilibrium measurements. The two archaebacteria investigated were Halobacterium cutirubrum, an extreme halophile, and Methanobacterium thermoautotrophicum, a thermophile which also showed properties of a moderate halophile. The changes in the secondary structure and the thermostability of these proteins were directly related to the internal salt concentrations of the two archaebacteria. At the higher salt concentrations the changes in the secondary structure resulted in changes in the tertiary and quaternary structure of these proteins.

scholarly journals The concerted inactivation of Escherichia coli uridine diphosphate galactose 4-epimerase by sugar nucleotide together with a free sugar

1976 ◽  
Vol 155 (2) ◽  
pp. 225-229 ◽  
Author(s):  
P Blackburn ◽  
W Ferdinand
Keyword(s):  
Escherichia Coli ◽  
Free Sugar ◽  
Uridine Diphosphate ◽  
Hydroxymethyl Group ◽  
Free Sugars ◽  
Sugar Nucleotides ◽  
Sugar Nucleotide ◽  
First Order ◽  
First Order Kinetics ◽  
Uridine Diphosphate Galactose

1. The combined effect of the sugar nucleotides UDP-D-fucose or UDP-D-glucuronic acid together with the free sugars D-fucose or L-arabinose is the inactivation of the Escherichia coli enzyme UDP-galactose 4-epimerase (EC 5.1.3.2). The sugar nucleotide or the free sugar alone or the sugar nucleotide plus 5'-Ump do not inactivate the enzyme. 2. The inactivation of the enzyme by its substrate UDP-D-glucose was not affected by the presence of free sugar. 3. In all cases the inactivation observed follows pseudo-first-order kinetics. 4. A comparison of various sugar nucleotides indicates that the hydroxymethyl group at position 6 of the sugar moiety of the natural substrates is important for substrate binding.

scholarly journals Competitive inhibition and substrate activity of uridine diphosphate 6-deoxygalactose for Escherichia coli uridine diphosphate galactose 4-epimerase (Short Communication)

1973 ◽  
Vol 131 (2) ◽  
pp. 421-423 ◽  
Author(s):  
M. Spencer ◽  
P. Blackburn ◽  
W. Ferdinand ◽  
G. M. Blackburn
Keyword(s):  
Escherichia Coli ◽  
Short Communication ◽  
Competitive Inhibition ◽  
Uridine Diphosphate ◽  
Uridine Diphosphate Galactose

UDP-6-deoxygalactose inhibits the UDP-galactose 4-epimerase (EC 5.1.3.2) from Escherichia coli in a competitive manner with respect to the substrate UDP-galactose, giving Ki 1.3×10-3m. As a substrate for the enzyme, it is transformed into UDP-6-deoxyglucose, although the reaction stops before equilibrium is attained. Possible causes of this behaviour are discussed.

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