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Bacterial sucrose isomerases: properties and structural studies
Biologia (Poland), 2008 International audienceDue to their significant role in food industry, sucrose isomerases are good candidates for rational protein engineering. Hence, specific modi.
Moez Rhimi +2 more
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Intracellular Trafficking, Localization, and Mobilization of Platelet-Borne Thiol Isomerases [PDF]
Arteriosclerosis, Thrombosis, and Vascular Biology, 2016 OBJECTIVE: Thiol isomerases facilitate protein folding in the endoplasmic reticulum, and several of these enzymes, including protein disulfide isomerase and ERp57, are mobilized to the surface of activated platelets, where they influence platelet ...
Marilena Crescente +2 more
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Borate and phosphoglucose isomerase in the assay of phosphomannose isomerase
Biochimica et Biophysica Acta, 1957Abstract The isomerization catalyzed by phosphohexose isomerases is essentially irreversible in the presence of excess borate, which selectively complexes with fructose-6-phosphate. This trapping effect gives zero order kinetics as long as there is enough substrate to saturate the enzyme.
F, ALVARADO, A, SOLS
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Cloning and overexpression of rhamnose isomerase and fucose isomerase
Bioorganic & Medicinal Chemistry, 1995Rhamnose isomerase and fucose isomerase were overexpressed in E. coli, purified and characterized. The rhamnose isomerase gene was ligated to the restriction sites of PstI and Hind III of vector pTrcHis and the fucose isomerase gene was ligated to the EcoRI and PstI sites of vector pKK223-3 for overexpression of the enzymes in E.
E, Garcia-Junceda +3 more
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Biochemistry, 2011
Understanding the catalytic efficiency and specificity of enzymes is a fundamental question of major practical and conceptual importance in biochemistry. Although progress in biochemical and structural studies has enriched our knowledge of enzymes, the role in enzyme catalysis of residues that are not nearest neighbors of the reacting substrate ...
Srinivas, Somarowthu +5 more
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Understanding the catalytic efficiency and specificity of enzymes is a fundamental question of major practical and conceptual importance in biochemistry. Although progress in biochemical and structural studies has enriched our knowledge of enzymes, the role in enzyme catalysis of residues that are not nearest neighbors of the reacting substrate ...
Srinivas, Somarowthu +5 more
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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 +3 more
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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 +3 more
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Studies on methylmalonyl isomerase
Biochimica et Biophysica Acta, 1962The 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", 1995L-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, 1992Several 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 +4 more
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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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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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