R73A and H144Q mutants of the yeast mitochondrial cyclophilin Cpr3 exhibit a low prolyl isomerase activity in both peptide and protein-folding assays

FEBS Letters

Volumn 443, Issue 3, 1999, Pages 367-369

  Scholz, Christian ^a   Maier, Peter ^a   Dolinski, Kara ^b   Heitman, Joseph ^b   Schmid, Franz X ^a  

^a UNIVERSITY OF BAYREUTH   (Germany)

^b HOWARD HUGHES MEDICAL INSTITUTE   (United States)

Author keywords

Cyclophilin; Immunophilin; Mitochondrion; Prolyl isomerization; Protein folding

Indexed keywords

CYCLOPHILIN; IMMUNOPHILIN; ISOMERASE;

ARTICLE; ASSAY; ENZYME ACTIVITY; MITOCHONDRION; MUTANT; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; YEAST;

ARGININE; BINDING SITES; CARRIER PROTEINS; CHROMATOGRAPHY; CHYMOTRYPSIN; CIRCULAR DICHROISM; CYCLOSPORINE; ESCHERICHIA COLI PROTEINS; HISTIDINE; HUMANS; KINETICS; MITOCHONDRIA; MUTATION; PEPTIDYLPROLYL ISOMERASE; PROTEIN BINDING; PROTEIN FOLDING; RECOMBINANT FUSION PROTEINS; SACCHAROMYCES CEREVISIAE; SUBSTRATE SPECIFICITY; TACROLIMUS;

ESCHERICHIA COLI;

EID: 0033062255     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(98)01735-9     Document Type: Article

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