Plant biosynthetic enzymes rapidly evolve to catalyze specialized reactions. Here, the authors present the crystal structure and mechanism of COSY, the enzyme involved in coumarin biosynthesis of the BAHD-acyltransferase family that catalyzes an intramolecular acyl transfer reaction through a proton exchange...
any of a class of enzymes that catalyze reactions involving intramolecular rearrangements. [1940–45] Random House Kernerman Webster's College Dictionary, © 2010 K Dictionaries Ltd. Copyright 2005, 1997, 1991 by Random House, Inc. All rights reserved. ...
Intramolecular oxidoreductases catalyze the oxidation-reduction reactions within a single molecule, resulting in the rearrangement of bonds. An example isglucose-6-phosphate isomerase, which converts glucose-6-phosphate to fructose-6-phosphate in the glycolytic pathway. ...
The invention provides human isomerases (ISOM) and polynucleotides which identify and encode ISOM. The invention also provides expression vectors, host cells, antibodies, agonists, and antagonists. The invention also provides methods for diagnosing, treating, or preventing disorders associated with aberran...
Chaperones suppress non-productive side reactions by stoichiometric binding to folding intermediates, and folding enzymes catalyze slow rate-limiting steps of folding. We reinvestigated, whether peptidyl-prolyl-cis/trans-isomerases of the cyclophilin type act simultaneously as chaperones and as folding ...
Their catalytic activity is extremely highmdash;the rate constants for the bimolecular reactions they catalyze approach the diffusion-controlled limit for enzyme-substrate reactions. These enzymes increase the rate of isomerization in oligopeptides as well as in intermediate in protein folding. It is ...
WorkonhumanandotheranimalPDIsshowsthatPDI belongs to the thioredoxin (TRX) protein super-family, which catalyzes cellular redox reactions (Holm-gren 1985), and interacts with nascent polypeptides tocatalyze the formation and isomerization of disulphidebonds (Creighton et al. 1980). The secondary struc...
Protein-disulfide isomerase is essential for formation and reshuffling of disulfide bonds during nascent protein folding in the endoplasmic reticulum. The two thioredoxin-like active sites catalyze a variety of thiol-disulfide exchange reactions. We have characterized three novel protein-disulfide isomerases...