Disease relevance of ECs4709

• On the other hand, Suc-Ala-Ser-4(S)-FPro-Phe-pNA exhibits a discriminating specificity toward the prototypic parvulin, the Escherichia coli Par10 [1].

High impact information on ECs4709

• Here we show that a variant of SurA lacking both parvulin-like domains exhibits a PPIase-independent chaperone-like activity in vitro and almost completely complements the in vivo function of intact SurA [2].
• Partial sequence analysis of the purified enzyme (DlPar13) revealed sequence homology to members of the parvulin family of PPIases [3].
• The mode of action was studied by analyzing the inactivation kinetics and the nature of products of the reaction of E. coli parvulin and its Cys69Ala variant with juglone [4].
• In contrast to FK506 binding proteins and cyclophilins, the parvulin family of peptidyl-prolyl cis/trans isomerases (PPIases; E.C. 5.2.1.8) cannot be inhibited by either FK506 or cyclosporin A [4].
• A second member of the parvulin family of peptidyl-prolyl cis/trans isomerases was identified in a human lung cDNA library [5].

Biological context of ECs4709

• Confirmation of the existence of a third family among peptidyl-prolyl cis/trans isomerases. Amino acid sequence and recombinant production of parvulin [6].
• The longer Parvulin protein is encoded by the human genome but absent from rodent, bovine and non-mammalian genomes [7].

Associations of ECs4709 with chemical compounds

• Selective inactivation of parvulin-like peptidyl-prolyl cis/trans isomerases by juglone [4].

Analytical, diagnostic and therapeutic context of ECs4709

• RESULTS: In this study we confirm by RT-PCR the existence of a longer Parvulin isoform expressed in all tissues examined so far [7].
• About 1% of all Parvulin mRNAs include the novel extension as quantified by real-time PCR [7].

References