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Spectral changes arising from the action of spinach chloroplast ribose phosphate isomerase ec 5.3.1.6 on ribose 5 phosphate


, : Spectral changes arising from the action of spinach chloroplast ribose phosphate isomerase ec 5.3.1.6 on ribose 5 phosphate. Archives of Biochemistry and Biophysics 202(1): 106-115

Following addition of spinach chloroplast ribosephosphate isomerase (RPI) to ribose 5-phosphate (R5P) buffered with neutral phosphate, the sequential appearance of compounds absorbing at 280, 308.5 and 285 nm was observed. The 280 nm absorbing compound has prevously been identified as ribulose 5-phosphate (Ru5P). The 308.5 nm absorbing compound has a high molar extinction coefficient and was a transient species, appearing only after production of Ru5P and preceding the accumulation of the 285 nm absorbing compound. The 285-nm absorbing compound has been identified as 4-hydroxy-5-methyl-2(3H)-furanone (I). Following addition of rabbit skeleton muscle RPI to R5P buffered with phosphate only the 280-nm absorbing compound, Ru5P, could be observed. Preparations of RPI from photosynthetic tissues have invariably led to the rapid accumulation of I whereas preparations of RPI from nonphotosynthetic tissues produce only Ru5P. In solutions of R5P buffered with citrate, the transient band at 308.5 nm was not observed although I accumulates in solution in the presence of spinach chloroplast RPI. Prior to formation of I a compound with a low molar extinction coefficient and wavelength of maximum absorption at approximately 310 nm can be detected. Apparently, purified preparations of RPI from spinach chloroplasts and other photosynthetic tissues possess an enzymatic activity not present in crude extracts obtained from non-photosynthetic tissues. This activity is in addition to the aldol-ketol activity. The product of this heretofore unrecognized enzymic activity is postulated to be 3,4-epoxy-Ru5P and could be derived from Ru5P by removing the elements of water from the hydroxyl groups at C-3 and C-4.

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Related references

Knowles, F.C.; Chanley, J.D.; Pon, N.G., 1980: Spectral changes arising from the action of spinach chloroplast ribosephosphate isomerase on ribose 5-phosphate. Following addition of spinach chloroplast ribosephosphate isomerase (RPI) to ribose 5-phosphate (R5P) buffered with neutral phosphate, the sequential appearance of compounds absorbing at 280, 308.5, and 285 nm was observed. The 280-nm absorbing co...

Knowles F.C., 1973: Discovery of an enzymic transformation of ribulose 5 phosphate to a compound other than ribose 5 phosphate or xylulose 5 phosphate by ribose phosphate isomerase from spinach chloroplasts. Plant Physiology (Rockville) 51(SUPPL): 41

Chandrasekaran B.; Ardalan B., 1983: Separation of ribose 5 phosphate ribose 1 phosphate deoxy ribose 1 phosphate by high performance liquid chromatography and spectrometric determination using 2 cyano acetamide/. A simple procedure for separation of ribose-5-phosphate, deoxyribose-1-phosphate and ribose-1-phosphate is based on high performance liquid chromatography using a reversed phase 4 .times. 300 mm .mu.Bondapak/NH2 column. The column is equilibrated...

Sindelar L.; Sindelarova M., 1987: Changes in ribose phosphate isomerase and ribose phosphate pyrophosphokinase activities in tobacco infected with pvy. Changes in ribosephosphate isomerase and ribosephosphate pyrophosphokinase activities occurring in tobacco leaf tissues infected with the potato virus Y (PVY) were studied at the stage of acute infection. The results obtained have shown that durin...

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Ivanishchev V.V.; Nasyrov Y.S.; Akhmedov Y.D., 1982: Some physicochemical properties of ribose 5 phosphate isomerase ec 5.3.1.6 from spinach leaves. An electrophoretically homogenous D-ribose-5-phosphate-ketol-isomerase (EC 5.3.1.6) from spinach leaves was obtained. The effects of substrate, temperature, pH and some agents on the enzyme activity were studied and the kinetic parameters were cal...

Jung, C.H.; Lu, T.Y.S.; Larimer, F.W., 1998: Heterologous expression and characterization of ribose-5-phosphate isomerase from spinach. FASEB Journal 12(8): A1450, April 24

Ivanishchev, V.V.; Akhmedov, I.D.; Nasyrov, I.S., 1982: Physico-chemical properties of ribose-5-phosphate isomerase from spinach leaves. An electrophoretically homogenous D-ribose-5-phosphate-ketol-isomerase (Ec 5.3.1.6) from spinach leaves was obtained. The effects of substrate, temperature, pH and some agents on the enzyme activity were studied and the kinetic parameters were cal...

Knowles, Francis-Charles, 1968: Enzymic transformations of D-ribose-5-phosphate by spinach leaf ribosephosphate isomerase

Anonymous, 1974: Simple procedures for the preparation of d ribose 5 phosphate ketol isomerase ec 5316 d ribulose 5 phosphate 3 epimerase ec 5131 and d sedo heptulose 7 phosphate d glyceraldehyde 3 phosphate glycolaldehyde transferase ec 2211