Results 211 to 220 of about 11,574 (255)

Prolyl isomerases in yeast

Frontiers in Bioscience, 2004
Prolyl isomerases are enzymes that catalyze cis-trans isomerization of peptidyl-prolyl bonds and span three structurally unrelated protein families: the cyclophilins, FKBPs, and parvulins. The genome of the budding yeast Saccharomyces cerevisiae encodes eight different cyclophilins (Cpr1 to Cpr8), four FKBPs (Fpr1 to Fpr4), and a single parvulin (Ess1).
Miguel, Arevalo-Rodriguez, Xiaoyun, Wu, Steven D, Hanes, Joseph, Heitman   +3 more
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Studies on methylmalonyl isomerase

Biochimica et Biophysica Acta, 1962
The partial purification (approx. 23-fold) and assay of the methylmalonyl isomerase system from bovine-liver mitochondria is described. The purified isomerase system catalyzes the isomerization of enzymically-synthesized [1-14C]- and [3-14C]methyl-malonyl-CoA to form [1-14C]- and [4-14C]succinyl-CoA, respectively. This is in agreement with the proposal
C S, HEGRE, S J, MILLER, M D, LANE
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The evolution of sugar isomerases

"Protein Engineering, Design and Selection", 1995
L-Arabinose isomerase (EC 5.3.1.4) catalyzes the isomerization of L-arabinose to L-ribulose. Here we report on the purification, kinetic mechanism and chemical mechanism of L-arabinose isomerase from Escherichia coli. The enzyme catalyzes the isomerization of L-arabinose to L-ribulose by a proton transfer mechanism, in contrast to xylose isomerase ...
S, Banerjee, F, Anderson, G K, Farber
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Isomerase and Chaperone Activity of Prolyl Isomerase in the Folding of Carbonic Anhydrase

Science, 1992
Several proteins have been discovered that either catalyze slow protein-folding reactions or assist folding in the cell. Prolyl isomerase, which has been shown to accelerate rate-limiting cis-trans peptidyl-proline isomerization steps in the folding pathway, can also participate in the protein-folding process as a ...
P O, Freskgård, N, Bergenhem, B H, Jonsson, M, Svensson, U, Carlsson   +4 more
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Comparative inactivation and inhibition of the anomerase and isomerase activities of phosphoglucose isomerase

Molecular and Cellular Biochemistry, 1981
Several metabolic compounds have been found to be competitive inhibitors of the anomerase activity of phosphoglucose isomerase (EC 5.3.1.9).Ki values for erythrose 4-phosphate, 6-phosphogluconate, and fructose 1,6-bisphosphate for the anomerase reaction are 0.32 muM, 21 muM, and 84 muM respectively at 0 degree and pH 8.2.
E E, Howell, K J, Schray
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Immobilization of glucose isomerase

Zeitschrift für allgemeine Mikrobiologie, 1982
AbstractThe immobilization of glucose isomerase (D‐xylose ketol isomerase, EC 5.3.1.5) by covalently bonding to various carriers and by adsorption to ion exchange resins was attempted in order to obtain a stable immobilized enzyme which can be used for continuous isomerization of glucose in a column.Of the covalent bonding methods, the colloidal silica‐
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Thermoinactivation mechanism of glucose isomerase

Applied Biochemistry and Biotechnology, 2007
In this article, the mechanisms of thermoinactivation of glucose isomerase (GI) from Streptomyces rubiginosus (in soluble and immobilized forms) were investigated, particularly the contributions of thiol oxidation of the enzyme's cysteine residue and a "Maillard-like" reaction between the enzyme and sugars in high fructose corn syrup (HFCS). Soluble GI
Leng Hong, Lim, Bradley A, Saville
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The determination of triosephosphate isomerase

Archives of Biochemistry and Biophysics, 1956
Abstract The difference in rate of formation of the chromogenic 2,4-dinitrophenylosazone derivatives of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate permits accurate measurement of the two triose phosphates in a mixture by means of carefully timed chromogen development reactions.
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Aconitate isomerase

Biochemical and Biophysical Research Communications, 1961
M R, RAO, W W, ALTEKAR
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Oxidative Cysteine Modification of Thiol Isomerases in Thrombotic Disease: A Hypothesis

Antioxidants and Redox Signaling, 2021
Moua Yang, Robert Flaumenhaft
exaly