Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.26 (invertase)
 4,927 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. The pH-activity relationship of invertase has been studied in vivo and in vitro under identical external environmental conditions. 2. The effect of changing (H(+)) upon the sucroclastic activity of living cells of S. cerevisiae and of invertase solutions obtained therefrom has been found, within experimental error, to be identical. 3. The region of living yeast cells in which invertase exerts its physiological activity changes its pH freely and to the same extent as that of the suspending medium. It is suggested that this may indicate that this intracellular enzyme may perform its work somewhere in the outer region of the cell. 4. In using live cells containing maltase, no evidence of increased sucroclastic activity around pH 6.9, due to the action of Weidenhagen's alpha-glucosidase (maltase), was found.
J Gen Physiol 1932 Nov 20
PMID:SIMILARITY OF THE KINETICS OF INVERTASE ACTION IN VIVO AND IN VITRO. II. 1987 2

1. The relationship of sucrose and water concentration to invertase activity in vivo and in vitro has been studied under the same environmental conditions. 2. The sucroclastic activity of S. cerevisiae cells and of invertase solutions prepared from them reacts to changes in sucrose and water concentration in an identical manner. 3. The invertase contained in living yeast cells is just as freely exposed to the conditions of sucrose and water concentrations of the suspending medium as it would be if it were contained in a cell-free solution. Weight is added to the previous suggestion (2) that yeast invertase exerts its physiological activity in a region quite close to the surface of the cell.
J Gen Physiol 1933 Mar 20
PMID:SIMILARITY OF THE KINETICS OF INVERTASE ACTION IN VIVO AND IN VITRO. III. 1987 22

Inversion of sucrose by bakers' yeast follows the same course as inversion catalyzed by yeast invertase. Rate of inversion increases exponentially with temperature; the temperature characteristic in the Arrhenius equation is 10,700 below 13-17 degrees C., and 8,300 above that temperature. Temperature inactivation occurs above 40 degrees C. The effects of temperature upon rate of inversion were the same using Fleischmann's yeast cake, the same yeast killed with toluene, and a pure strain (G. M. No. 21062) of bakers' yeast. The last differed from the other two only in the fact that its critical temperature was 13 degrees C. as compared with 17 degrees C. for the others. The catalytic inversion is associated with enzyme activity inside the cell, not in the medium, and is independent of any vital processes inside the cell such as respiration and fermentation. Since invertase activity is the same inside the cell as it is after extraction, it appears possible to relate the temperature characteristics for physiological processes to the catalytic chemical systems which determine their rate. At least two enzymes are capable of inverting sucrose in the yeast cell. The familiar yeast invertase (micro = 10,700) is active below 13-17 degrees C. while a second enzyme (M = 8,300) plays the dominant role above that temperature.
J Gen Physiol 1938 Jul 20
PMID:SUCROSE INVERSION BY BAKERS' YEAST AS A FUNCTION OF TEMPERATURE. 1987 76

1. Acid-inactivated yeast invertase could not be regenerated in the presence of the proteolytic enzymes trypsin, pepsin, and chymotrypsin. 2. Certain foreign proteins of non-enzymatic nature partially inhibited the reactivation of acid-inactivated invertase. 3. Certain proteins as gelatin, lacto-globulin, and carbohydrate-free horse crystalbumin did not prevent the reactivation of invertase at all. 4. Highly purified reactivated invertase was shown to exhibit an effect typical of original native invertase; that is, acceleration of its activity in presence of foreign protein at pH 3.0. 5. Native invertase was not digested by trypsin and chymotrypsin. 6. The addition of trypsin and chymotrypsin to reactivating invertase did not affect the invertase which had already reverted to the active form, but prevented further reactivation of inactive invertase.
J Gen Physiol 1941 Nov 20
PMID:THE INFLUENCE OF PROTEINS ON THE REACTIVATION OF YEAST INVERTASE. 1987 66

The activity of yeast invertase as a function of oxidation-reduction potential has been investigated using a large number of oxidants and reductants. The activity is constant over the range of E(h) from -270 to +600 mv., but above E(h) = +600 mv. there is a sharp decrease in activity reaching 0 at E(h) = +1,000 mv. The inhibiting action of strong oxidants is upon the enzyme rather than on the substrate and appears to be essentially irreversible Experiments indicate that the inhibiting action of strong oxidants on invertase is primarily related to their high oxidation-reduction potential rather than to a specific toxic action unrelated to E(h). The effects of oxidation-reduction potential upon invertase activity are independent of the purity of the enzyme, since they are the same for commercial invertases, fresh bakers' yeast, powdered bakers' yeast, brewers' yeast, and highly purified invertase. Possible mechanisms involved in the inactivation of invertase by oxidants are discussed.
J Gen Physiol 1942 Jan 20
PMID:THE ACTIVITY OF YEAST INVERTASE AS A FUNCTION OF OXIDATION-REDUCTION POTENTIAL. 1987 83

The lower leaves of tobacco plants were inoculated with leaf mosaic virus and the activities of oxygenase, peroxidase, catalase, and invertase were followed in leaves of comparable age at intervals of 2 or 3 days over a period of 21 days. The inoculated leaves exhibited a great decrease relative to normal tissue in the activity of oxygenase and peroxidase on the 6th day. Younger leaves showed this minimum at a progressively later date. A great decrease in the activities of these enzymes was attained by the 14th to the 18th day. This maximum was followed by a decrease. Catalase exhibited an increased activity which reached a maximum at about the 8th day. A second maximum was observed on the 16th to the 18th day. Invertase reached a minimum, relative to normal plants, on about the 8th day. A second minimum was approached on the 16th to the 18th day. These data show that profound disturbances in the physiology of infected plants occur many days before the leaf juice attains an infectious concentration of virus. The observed activities could not be due therefore to metabolic activities of the virus particles themselves. Since infectivity is attained only after a period of profound physiological disturbance, it seems possible that the virus protein develops as a product of abnormal metabolism.
J Gen Physiol 1942 Mar 20
PMID:CERTAIN ENZYMATIC ACTIVITIES OF NORMAL AND MOSAIC INFECTED TOBACCO PLANTS. 1987 2

1. Some 16 amino acids (not containing SH or S-S groups) did not affect the reactivation of yeast invertase inactivated by acid. 2. Cysteine, reduced glutathione, homocysteine, thiophenol, and thioglycollic acid accelerated the reactivation of yeast invertase. 3. Cystine, oxidized glutathione, and homocystine inhibited the reactivation of yeast invertase. 4. The compounds mentioned in 2 and 3 did not affect native invertase. 5. The use of compounds in which the H of the SH group of homocysteine was substituted by a methyl or benzyl nullified the accelerative effect. 6. The longer the cysteine remained in contact with the inactivating enzyme, the greater was the velocity of the reactivated invertase. 7. The per cent acceleration by cysteine is inversely proportional to the control rate.
J Gen Physiol 1943 May 20
PMID:THE INFLUENCE OF AMINO ACIDS ON THE REACTIVATION OF YEAST INVERTASE. 1987 60


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