2009
DOI: 10.1002/pro.28
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A nonessential role for Arg 55 in cyclophilin18 for catalysis of proline isomerization during protein folding

Abstract: The protein folding process is often in vitro rate-limited by slow cis-trans proline isomerization steps. Importantly, the rate of this process in vivo is accelerated by prolyl isomerases (PPIases). The archetypal PPIase is the human cyclophilin 18 (Cyp18 or CypA), and Arg 55 has been demonstrated to play a crucial role when studying short peptide substrates in the catalytic action of Cyp18 by stabilizing the transition state of isomerization. However, in this study we show that a R55A mutant of Cyp18 is as ef… Show more

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Cited by 10 publications
(10 citation statements)
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“…A similar scenario likely occurs also with CyP33 (PPIE), because its PPIase activity is stimulated upon specific binding of mRNA (Wang et al, 2008). By contrast, the chaperone activity of PPIase-deficient CyPA is inhibited by CsA in a model substrate (Moparthi et al, 2010; Moparthi et al, 2009). …”
Section: Immunophilins' Role(s) and Beyondmentioning
confidence: 94%
See 1 more Smart Citation
“…A similar scenario likely occurs also with CyP33 (PPIE), because its PPIase activity is stimulated upon specific binding of mRNA (Wang et al, 2008). By contrast, the chaperone activity of PPIase-deficient CyPA is inhibited by CsA in a model substrate (Moparthi et al, 2010; Moparthi et al, 2009). …”
Section: Immunophilins' Role(s) and Beyondmentioning
confidence: 94%
“…In this regard, the enzymatic proficiency of cyclophilins compared to that of other enzymes is arguably low (Radzicka and Wolfenden, 1995). Further, it was shown recently with model substrates that there was no difference in the acceleration of refolding of carbonic anhydrase II in vitro between wild-type (CyPA\PPIA) and a mutant without PPIase activity, CyPA (R55A) (Moparthi et al, 2009). CyPA also acts as a chaperone in vitro by functioning as a hydrophobic basket toward misfolding-prone regions of model substrates, such as carbonic anhydrase II, creatin kinase and citrate synthase (Moparthi et al, 2010; Ou et al, 2001).…”
Section: Historical Overview Of Ninaa Genementioning
confidence: 99%
“…Mutations at the active site of Cpr3 dramatically reduce the PPIase activities toward both peptide and protein (RNase T 1 ) substrates. However, a contrary result has been reported for hCyp18 [41]. Mutation at Arg55 of hCyp18 dramatically reduces PPIase pep activity without seriously affecting PPIase pro activity.…”
Section: Resultsmentioning
confidence: 83%
“…Active site residues in AquaCyp are only partially conserved to other cyclophilins. The residues Arg65 and Gln73 of AquaCyp293 correspond to Arg55 and Gln63 in hCyp18 and are essential for catalysis [ 46 48 ]. At other positions in the active site, the sequence conservation is lower.…”
Section: Resultsmentioning
confidence: 99%