BIOMAT Database Logo BIOMAT Database Logo

Interaction of uridine diphosphate glucose analogs with calf liver uridine diphosphate glucose dehydrogenase. Influence of substituents at C-5 of pyrimidine nucleus. 1975

V N Shibaev, and G I Eliseeva, and N K Kochetkov

The interaction of alpha-D-glucopyranosyl pyrophosphates of 5-X-uridines (X = CH3, NH2, CH3O, I, Br, Cl, OH) with uridine diphosphate glucose (UDPGlc) dehydrogenase (EC 1.1.1.22) from calf liver has been studied. All the derivatives investigated were able to serve as substrates for the enzyme. The apparent Michaelis constants for UDPGlc-analogs were dependent both on electronic and steric factors. Increase of substituent negative inductive effect lead to decrease of pKa for ionization of the NH-group in the uracil nucleus and, consequently, to a diminishing of the proportion of the active analog species under the conditions of assay. After correction for the ionization effect, the Km values were found to depend on the van der Waals radius of the substituent. The value of 1.95 A seems to be critical, as the analogs with bulkier substituents at C-5 showed a decreased affinity to the enzyme. The maximal velocity values of the analogs were also dependent on nature of the substituent. Good linear correlation between log V and substituent hydrophobic phi-constant was observed for a number of the analogs, although V values for the nucleotides with X = H, OH or NH2 were higher than would be expected on the basis of the correlation. The significance of the results for understanding of the topography of UDPGlc dehydrogenase active site is discussed.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D002417 Cattle Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor. Beef Cow,Bos grunniens,Bos indicus,Bos indicus Cattle,Bos taurus,Cow,Cow, Domestic,Dairy Cow,Holstein Cow,Indicine Cattle,Taurine Cattle,Taurus Cattle,Yak,Zebu,Beef Cows,Bos indicus Cattles,Cattle, Bos indicus,Cattle, Indicine,Cattle, Taurine,Cattle, Taurus,Cattles, Bos indicus,Cattles, Indicine,Cattles, Taurine,Cattles, Taurus,Cow, Beef,Cow, Dairy,Cow, Holstein,Cows,Dairy Cows,Domestic Cow,Domestic Cows,Indicine Cattles,Taurine Cattles,Taurus Cattles,Yaks,Zebus
D000429 Alcohol Oxidoreductases A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99). Carbonyl Reductase,Ketone Reductase,Carbonyl Reductases,Ketone Reductases,Oxidoreductases, Alcohol,Reductase, Carbonyl,Reductase, Ketone,Reductases, Carbonyl,Reductases, Ketone
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D013329 Structure-Activity Relationship The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups. Relationship, Structure-Activity,Relationships, Structure-Activity,Structure Activity Relationship,Structure-Activity Relationships
D014532 Uridine Diphosphate Glucose A key intermediate in carbohydrate metabolism. Serves as a precursor of glycogen, can be metabolized into UDPgalactose and UDPglucuronic acid which can then be incorporated into polysaccharides as galactose and glucuronic acid. Also serves as a precursor of sucrose lipopolysaccharides, and glycosphingolipids. UDP Glucose,UDPG,Uridine Diphosphoglucose,Diphosphate Glucose, Uridine,Diphosphoglucose, Uridine,Glucose, UDP,Glucose, Uridine Diphosphate
D014533 Uridine Diphosphate Glucose Dehydrogenase An enzyme that catalyzes the oxidation of UDPglucose to UDPglucuronate in the presence of NAD+. EC 1.1.1.22. UDP Glucose Dehydrogenase,UDPG Dehydrogenase,Dehydrogenase, UDP Glucose,Dehydrogenase, UDPG,Glucose Dehydrogenase, UDP

Related Publications

V N Shibaev, and G I Eliseeva, and N K Kochetkov
Interaction of uridine diphosphate glucose with calf liver uridine diphosphate glucose dehydrogenase. Significance of hydroxyl groups at C-3, C-4 and C-6 of hexosyl residue.
September 1975, Biochimica et biophysica acta,
V N Shibaev, and G I Eliseeva, and N K Kochetkov
Uridine diphosphate glucose dehydrogenase of calf liver. Properties and inhibition characteristics with uridine diphosphate xylose analogues.
September 1971, Biochemical pharmacology,
V N Shibaev, and G I Eliseeva, and N K Kochetkov
Interaction of nucleotides with liver uridine diphosphate-glucose-4'-epimerase.
February 1974, The Journal of biological chemistry,
V N Shibaev, and G I Eliseeva, and N K Kochetkov
URIDINE DIPHOSPHATE GLUCOSE DEHYDROGENASE. PH DEPENDENCE OF THE REACTIONS WITH THE 5-FLUOROURACIL AND 6-AZAURACIL ANALOGUES OF URIDINE DIPHOSPHATE GLUCOSE.
September 1963, The Journal of biological chemistry,
V N Shibaev, and G I Eliseeva, and N K Kochetkov
Half-sites oxidation of bovine liver uridine diphosphate glucose dehydrogenase.
August 1978, The Biochemical journal,
V N Shibaev, and G I Eliseeva, and N K Kochetkov
The interaction of adenosine diphosphate glucose and its synthetic analogs with uridine diphosphate glucose-fructose glucosyltransferase from pea seedlings.
January 1969, Biochimica et biophysica acta,
V N Shibaev, and G I Eliseeva, and N K Kochetkov
Uridine diphosphate glucose dehydrogenase of rat tissue.
October 1971, Biochimica et biophysica acta,
V N Shibaev, and G I Eliseeva, and N K Kochetkov
Histochemical demonstration of uridine diphosphate glucose dehydrogenase.
July 1961, Experientia,
V N Shibaev, and G I Eliseeva, and N K Kochetkov
[Mechanism of the enzymatic reaction catalyzed by uridine diphosphate glucose dehydrogenase. The chemical synthesis of uridine diphosphate glucose-6-H3 and its oxidation by uridine diphosphate glucose dehydrogenase].
January 1975, Biokhimiia (Moscow, Russia),
V N Shibaev, and G I Eliseeva, and N K Kochetkov
Uridine diphosphate glucose synthase from calf liver: determinants of enzyme activity in vitro.
December 1975, Biochemistry,
Copied contents to your clipboard!