Literature DB >> 15664856

Increased catalytic activity of protein disulfide isomerase using aromatic thiol based redox buffers.

Jonathan D Gough1, Watson J Lees.   

Abstract

PDI is an enzyme that acts as a chaperone, shufflase, and oxidase during the folding of disulfide-containing proteins. The ability of aromatic thiols to increase the activity of PDI-catalyzed protein folding over that of the standard thiol glutathione (GSH) was measured. 4-Mercaptobenzoic acid (ArSH) increased the activity of PDI by a factor of three.

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Year:  2005        PMID: 15664856     DOI: 10.1016/j.bmcl.2004.11.005

Source DB:  PubMed          Journal:  Bioorg Med Chem Lett        ISSN: 0960-894X            Impact factor:   2.823


  1 in total

1.  Organocatalysts of oxidative protein folding inspired by protein disulfide isomerase.

Authors:  John C Lukesh; Kristen A Andersen; Kelly K Wallin; Ronald T Raines
Journal:  Org Biomol Chem       Date:  2014-11-21       Impact factor: 3.876

  1 in total

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