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• W1536702702 abstract "Abstract 1. Formation of 11 sugar nucleotides from the respective nucleoside triphosphates and sugar 1-phosphates have been demonstrated with the crude extract of Azotobacter vinelandii. These are adenosine diphosphate glucose, cytidine diphosphate glucose, uridine diphosphate glucose, deoxythymidine diphosphate glucose, adenosine diphosphate N-acetylglucosamine, uridine diphosphate N-acetylglucosamine, deoxythymidine diphosphate N-acetylglucosamine, adenosine diphosphate glucosamine, cytidine diphosphate glucosamine, uridine diphosphate glucosamine, and deoxythymidine diphosphate glucosamine. 2. The CDP-glucose pyrophosphorylase activity has been resolved into two peaks (Fractions I and II) by diethylaminoethyl cellulose chromatography. 3. One of these fractions (Fraction I: Michaelis constant (Km) for cytidine triphosphate = 3.3 x 10-3 m) is accompanied by a predominant UDP-glucosamine pyrophosphorylase activity (Km for uridine triphosphate = 1.9 x 10-4 m), and the ratio of the two activities (1:26) did not vary during the purification and inactivation at 50°. It seems likely that both activities are catalyzed by the same enzyme. 4. Another fraction (Fraction II) has been purified 195-fold. The purified enzyme is specific for both nucleoside triphosphate and sugar 1-phosphate except glucosamine 1-phosphate, which is active in replacing the glucose 1-phosphate. The pH optimum of the reaction is 8.5, and its equilibrium constant measured in the direction of CDP-glucose synthesis is 0.57. The enzyme absolutely requires Mg++ ions for activity. Variation of the Mg++ ion concentration relative to either pyrophosphate or CTP has a marked influence on the reaction velocity as well as Km values for the substrates. Km values calculated for pyrophosphate and CTP are 5.6 x 10-4 m and 7 x 10-4 m, respectively, when the molar ratio of MgCl2 to the substrate is 2:1. 5. The enzyme (Fraction II) is inhibited by its products, CDP-glucose and pyrophosphate. The inhibition by CDP-glucose is strictly competitive with respect to CTP, whereas that by pyrophosphate is noncompetitive. 6. Deoxythymidine triphosphate is a strong inhibitor of the enzyme (Fraction II). It is competitive with CTP only partially, indicating that dTTP combines with a site other than the CTP-binding site. 7. The cytidine nucleotides, isolated from A. vinelandii and tentatively identified as cytidine diphosphate 2-O-methyldeoxyaldose and its carboxylic acid ester, also inhibit the enzyme (Fraction II). Plots of percentage inhibition against inhibitor concentration give sigmoid curves." @default.
• W1536702702 created "2016-06-24" @default.
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• W1536702702 date "1966-03-01" @default.
• W1536702702 modified "2023-09-26" @default.
• W1536702702 title "Studies on Cytidine Diphosphate Glucose Pyrophosphorylase and Related Enzymes of Azotobacter vinelandii" @default.
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• W1536702702 doi "https://doi.org/10.1016/s0021-9258(18)96808-0" @default.
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• W1536702702 hasPublicationYear "1966" @default.
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