Freedman, Robert B. and Klappa, Peter and Ruddock, Lloyd W. (2002) Model peptide substrates and ligands in analysis of action of mammalian protein disulfide-isomerase. Methods in Enzymology, 348 . pp. 342-354. ISSN 0076-6879. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)
Protein disulfide-isomerase (PDI) polypeptide comprises four distinct but homologous domains can function alone, as homo-oligomers, or as an obligatory component of hetero-oligomeric species, such as prolyl-4-hydroxylase and microsomal triglyceride transfer protein. Thus, PDI is a complex enzyme that catalyzes a complex reaction. Advances in understanding the action of this complex enzyme have come from three directions: (1) the definition of the domain structure of the PDI polypeptide; (2) the definition and validation of “partial reactions” with simple substrates, representing specific elements of the overall reaction catalyzed by PDI on its complex physiological substrates; and (3) the combination of these inputs to express recombinant PDI constructs comprising individual domains, combinations of domains or active-site mutant species, and to characterize them in functional terms. This chapter focuses on the second of these advances, describing peptide substrates for partial reactions of PDI and their use to define the overall catalytic process and to establish the roles within it of individual domains of PDI.
|Subjects:||Q Science > Q Science (General)|
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences > Protein Science Group|
|Depositing User:||Peter Klappa|
|Date Deposited:||04 Sep 2008 13:52|
|Last Modified:||16 Jun 2014 13:53|
|Resource URI:||https://kar.kent.ac.uk/id/eprint/3960 (The current URI for this page, for reference purposes)|