The activity of uridine diphosphate glucose-d-fructose 6-phosphate 2-glucosyltransferase in leaves.
نویسنده
چکیده
1. By using EDTA in reaction mixtures it was possible to determine the activity of sucrose phosphate synthetase in freshly prepared leaf extracts without the complications caused by sucrose phosphatase. 2. EDTA was found also to increase the activity of sucrose phosphate synthetase by as much as 100%. 3. High sucrose phosphate synthetase activities were found in leaf preparations in which sucrose phosphatase was inhibited by EDTA. By contrast with previous reports, the activities were sufficient to allow sucrose synthesis in leaves during photosynthesis to occur via sucrose phosphate. 4. Sugar-cane plants having different rates of photosynthesis also had different activities of sucrose phosphate synthetase in their leaves. 5. It is suggested that the activity of sucrose phosphate synthetase in leaves may play a role in the control of the rate of photosynthesis.
منابع مشابه
PARTIAL PURIFICATION AND PROPERTIES OF L-GLUTAMINE: D-FRUCTOSE 6-P AMIDOTRANSFERASE FROM HUMAN PLACENTA
The first enzyme of the pathway for uridine diphosphate N-acetyl-D-glucosamine (UDPAG) biosynthesis i.e. L-glutamine: D-fructose 6-P amidotransferase (E.C. 2.6.1.16) was purified 52-fold from human placenta using methanol fractionation and column chromatography on DEAE-Sephadex A-50. The enzyme showed optimal activity in a broad range of pH from 5.8 to 7.8 in both phosphate and cacodylate ...
متن کاملSome Properties of Potato Tuber UDPGd-fructose-2-glucosyltransferase (E.C. 2.4.1.14) and UDPGd-fructose-6-phosphate-2-glucosyltransferase (E.C. 2.4.1.13).
Sucrose and sucrose 6-phosphate synthetase were isolated from potato tubers, partially purified and their properties studied. The sucrose synthetase showed optimum activity at 45 degrees and was inhibited competitively by ADP and some phenolic glucosides. The Ki's for these inhibitors were determined. Mg(2+) was found to activate this enzyme. Activity toward UDP-glucose or ADP-glucose formation...
متن کاملUridine diphosphate glucose breakdown is mediated by a unique enzyme activated by fructose 2,6-bisphosphate in Solanum tuberosum.
In the presence of inorganic phosphate, uridine 5'-diphosphate glucose (UDPG) is specifically hydrolyzed to glucose 1-phosphate and UDP by a unique enzyme, UDPG phosphorylase. The activity of the enzyme was maximally stimulated by fructose 2,6-bisphosphate, a regulatory metabolite recently discovered in both plants and animals, and by 2-phosphoglyceric acid. At 1 muM, fructose 2,6-bisphosphate ...
متن کاملPhosphate inhibition of spinach leaf sucrose phosphate synthase as affected by glucose-6-phosphate and phosphoglucoisomerase.
The inhibition patterns of inorganic phosphate (Pi) on sucrose phosphate synthase activity in the presence and absence of the allosteric activator glucose-6-P was studied, as well as the effects of phosphoglucoisomerase on fructose-6-P saturation kinetics with and without Pi. In the presence of 5 millimolar glucose-6-P, Pi was a partial competitive inhibitor with respect to both substrates, fru...
متن کاملBinding of substrates and modifiers to glucosamine synthetase.
1. The binding of substrates and effectors to glucosamine synthetase (l-glutamine-d-fructose 6-phosphate aminotransferase, EC 2.6.1.16) was studied by using the ligand to alter the denaturation rate of the enzyme. The free enzyme bound fructose 6-phosphate, glucose 6-phosphate and UDP-N-acetylglucosamine, but not glutamine, AMP or UTP. Glucose 6-phosphate and AMP increased the binding of UDP-N-...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Biochemical journal
دوره 105 3 شماره
صفحات -
تاریخ انتشار 1967