Archaeal peptidyl prolyl cis-trans isomerases PPIases

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Microbial peptidyl-prolyl cis/trans isomerases (PPIases): virulence factors and potential alternative drug targets.

Initially discovered in the context of immunomodulation, peptidyl-prolyl cis/trans isomerases (PPIases) were soon identified as enzymes catalyzing the rate-limiting protein folding step at peptidyl bonds preceding proline residues. Intense searches revealed that PPIases are a superfamily of proteins consisting of three structurally distinguishable families with representatives in every describe...

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Peptidyl-prolyl cis/trans isomerases and transcription: is there a twist in the tail?

Eukaryotic transcription is regulated predominantly by the post-translational modification of the participating components. One such modification is the cis-trans isomerization of peptidyl-prolyl bonds, which results in a conformational change in the protein involved. Enzymes that carry out this reaction include the yeast peptidyl-prolyl cis/trans isomerase Ess1 and its human counterpart Pin1, ...

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Insights into the catalytic mechanism of peptidyl prolyl cis/trans isomerases.

A large body of physiological, cell biological, kinetic and structural data about peptidyl prolyl cis/trans isomerases (PPIases) has been accumulated during the past 20 years, but despite the simplicity of the catalyzed reaction the question of how the enzyme action is performed is still not fully answered. In this review the center of attention is the molecular background of the catalytic mech...

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Determination of kinetic constants for peptidyl prolyl cis-trans isomerases by an improved spectrophotometric assay.

The kinetic properties and substrate specificity of two well-characterized peptidyl prolyl cis-trans isomerases (PPIases), cyclophilin and the FK-506 binding protein (FKBP), have been previously examined [Fischer, G., Bang, H., Berger, E., & Schellenberger, A. (1984) Biochim. Biophys. Acta 791, 87-97; Harrison, R.K., & Stein, R.L. (1990) Biochemistry 29, 1684-1689; Albers, M.W., Walsh, C.T., & ...

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Immunophilins and parvulins. Superfamily of peptidyl prolyl isomerases in Arabidopsis.

Immunophilins are defined as receptors for immunosuppressive drugs including cyclosporin A, FK506, and rapamycin. The cyclosporin A receptors are referred to as cyclophilins (CYPs) and FK506- and rapamycin-binding proteins are abbreviated as FKBPs. These two groups of proteins (collectively called immunophilins) share little sequence homology, but both have peptidyl prolyl cis/trans isomerase (...

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ژورنال

عنوان ژورنال: Frontiers in Bioscience

سال: 2000

ISSN: 1093-9946,1093-4715

DOI: 10.2741/a554