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During the maturation of extracellular proteins, disulfide bonds that chemically cross-link specific cysteines are often added to stabilize a protein or to join it covalently to other proteins. Disulfide formation, which requires a change in the covalent structure of the protein, occurs as the protein folds into its three-dimensional structure.
Bonney, Wilkinson, Hiram F, Gilbert
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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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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).
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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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