Erratum

You have free access to this content

A nonessential role for Arg 55 in cyclophilin18 for catalysis of proline isomerization during protein folding

  1. Satish Babu Moparthi,
  2. Per Hammarström,
  3. Uno Carlsson*

Article first published online: 26 MAY 2009

DOI: 10.1002/pro.129

Issue

Protein Science

Protein Science

Volume 18, Issue 6, page 1332, June 2009

Additional Information

How to Cite

Moparthi, S. B., Hammarström, P. and Carlsson, U. (2009), A nonessential role for Arg 55 in cyclophilin18 for catalysis of proline isomerization during protein folding. Protein Science, 18: 1332. doi: 10.1002/pro.129

Author Information

  1. IFM-Department of Chemistry, Linköping University, SE-581 83 Linköping, Sweden

*IFM-Department of Chemistry, Linköping University, SE-581 83 Linköping, Sweden

Publication History

  1. Issue published online: 26 MAY 2009
  2. Article first published online: 26 MAY 2009

SEARCH

SEARCH BY CITATION

ARTICLE TOOLS

Get PDF (35K)

Moparthi SB, Hammarström P, Carlsson U. (2009) Protein Sci 18:475–479. In this article the cited comparison (Ref. 21) that the mitochondrial cyclophilin Cpr3 with a homologous active-site R73A mutation retained its prolyl isomerase activity towards a protein substrate1 is not valid, since the activity has been reported to originate from a contamination of an E. coli protein SlyD2. Thus, human cyclophilin18 is so far the only cyclophilin that has been shown to be able to catalyze prolyl isomerization during protein folding without Arg55 that is essential for smaller peptide substrates.

1. Scholz C, Schindler T, Dolinski K, Heitman J, Schmid FX (1997) Cyclophilin active site mutants have native prolyl isomerase activity with a protein substrate. FEBS Lett 414:69–73.

2. Scholz C, Maier P, Dolinski K, Heitman J, Schmid FX (1999) R73A and H144Q mutants of the yeast mitochondrial cyclophilin Cpr3 exhibit a low prolyl isomerase activity in both peptide and protein-folding assays. FEBS Lett 443:367–369.

Get PDF (35K)