isomerase activity

Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5. [ISBN:0198506732… (More)
National Institutes of Health

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Isomerase

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Highly Cited
2011
Highly Cited
2011
Death-associated protein kinase 1 phosphorylates Pin1 and inhibits its prolyl isomerase activity and cellular function.
Pin1 is a phospho-specific prolyl isomerase that regulates numerous key signaling molecules and whose deregulation contributes to… (More)
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Highly Cited
2004
Highly Cited
2004
Rpe65 is a retinyl ester binding protein that presents insoluble substrate to the isomerase in retinal pigment epithelial cells.
Photon capture by a rhodopsin pigment molecule induces 11-cis to all-trans isomerization of its retinaldehyde chromophore. To… (More)
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2004
2004
Trigger factor peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli.
The ribosome-associated Trigger Factor (TF) cooperates with the DnaK system to assist the folding of newly synthesized… (More)
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Highly Cited
2003
Highly Cited
2003
Chloroplast cyclophilin is a target protein of thioredoxin. Thiol modulation of the peptidyl-prolyl cis-trans isomerase activity.
Chloroplast cyclophilin has been identified as a potential candidate of enzymes in chloroplasts that are regulated by thioredoxin… (More)
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2002
2002
Cyclophilin A peptidyl-prolyl isomerase activity promotes ZPR1 nuclear export.
The peptidyl-prolyl isomerase (PPIase) cyclophilin A (Cpr1p) is conserved from eubacteria to mammals, yet its biological function… (More)
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1999
1999
Identification of protein-disulfide isomerase activity in fibronectin.
Assembly and degradation of fibronectin-containing extracellular matrices are dynamic processes that are up-regulated during… (More)
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Highly Cited
1996
Highly Cited
1996
SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins.
Little is known about either the process of periplasmic protein folding or how information concerning the folding state in this… (More)
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1995
1995
Independence of the chaperone activity of protein disulfide isomerase from its thioredoxin-like active site.
Protein disulfide isomerase (PDI) alkylated at thiols of the thioredoxin-like -CHC- active sites is devoid of isomerase activity… (More)
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1992
1992
Protein disulfide isomerase activity is released by activated platelets.
The release of protein disulfide isomerase by activated platelets was hypothesized on the basis of reported intermolecular and… (More)
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1992
1992
Expression and site-directed mutagenesis of human protein disulfide isomerase in Escherichia coli. This multifunctional polypeptide has two independently acting catalytic sites for the isomerase…
Protein disulfide isomerase (PDI, EC 5.3.4.1) is a highly unusual multifunctional polypeptide, being identical to the beta… (More)
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