Structural and functional characterization of Escherichia coli peptidyl-prolyl cis-trans isomerases
نویسندگان
چکیده
منابع مشابه
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...
متن کاملPeptidyl-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, ...
متن کاملInsights 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...
متن کاملDetermination 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., & ...
متن کاملThe Escherichia coli SlyD is a metal ion-regulated peptidyl-prolyl cis/trans-isomerase.
In Escherichia coli as many as nine different genes coding for proteins with significant homology to peptidyl-prolyl cis/trans-isomerases (PPIases) have been found. However, for three of them, the histidine-rich SlyD, the homologous gene product of ORF149, and parvulin-like SurA, it was not known whether these proteins really possess PPIase activity. To gain access to the full set of PPIases in...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1992
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1992.tb17002.x