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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… Expand
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… Expand
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Highly Cited
2004
Highly Cited
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… Expand
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Highly Cited
2003
Highly Cited
2003
Biochemical and Functional Analyses of the Mip Protein: Influence of the N-Terminal Half and of Peptidylprolyl Isomerase Activity on the Virulence of Legionella pneumophila
ABSTRACT The virulence factor Mip (macrophage infectivity potentiator) contributes to the intracellular survival of Legionella… Expand
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Highly Cited
2000
Highly Cited
2000
The Platelet Integrin αIIbβ3 Has an Endogenous Thiol Isomerase Activity*
Integrins are cysteine-rich heterodimeric cell-surface adhesion molecules that alter their affinity for ligands in response to… Expand
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Highly Cited
1999
Highly Cited
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… Expand
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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… Expand
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Highly Cited
1995
Highly Cited
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… Expand
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Highly Cited
1993
Highly Cited
1993
Chlamydia trachomatis Mip‐like protein has peptidylprolyl cis/trans isomerase activity that is inhibited by FK506 and rapamycin and is implicated in initiation of chlamydial infection
The Mip‐like protein of Chlamydia trachomatis has sequence similarity with both the Mip protein of Legionella pneumophila, a… Expand
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Highly Cited
1992
Highly Cited
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… Expand
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Highly Cited
1992
Highly Cited
1992
A Pro to His mutation in active site of thioredoxin increases its disulfide-isomerase activity 10-fold. New refolding systems for reduced or randomly oxidized ribonuclease.
Thioredoxin (Trx) from Escherichia coli was compared with bovine protein disulfide-isomerase (PDI) for its ability to catalyze… Expand
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