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Natalya K Nagra Foldases Catalyzing the Formation & Isom (Paperback) (UK IMPORT)
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- Book Title
- Foldases Catalyzing the Formation and Isomerization of Disulfide Bonds in Proteins
- Publication Name
- Foldases Catalyzing the Formation & Isomerization of Disulfide Bo
- Title
- Foldases Catalyzing the Formation & Isomerization of Disulfide Bo
- Format
- Trade Paperback
- ISBN-10
- 1606924664
- EAN
- 9781606924662
- ISBN
- 9781606924662
- Publisher
- NOVA Science Publishers, Incorporated
- Genre
- Science
- Release Date
- 01/04/2009
- Release Year
- 2009
- Language
- English
- Country/Region of Manufacture
- US
- Item Height
- 140mm
- Item Length
- 5.5in
- Item Weight
- 5.7 Oz
- Publication Year
- 2009
- Topic
- Life Sciences / Biochemistry, Chemistry / Organic, Chemistry / General
- Item Width
- 8.5in
- Number of Pages
- 75 Pages
關於產品
Product Information
One of the rate-limiting steps in the folding pathways of many secretory proteins is the formation of correct disulfide bonds between cysteine residues. In eukaryotes, both disulfide bond formation and isomerisation which shuffles incorrectly formed disulfides are catalysed by protein disulfide isomerase (PDI), whereas in bacteria these two reactions are catalysed by separate enzymes. Both in eukaryotic and prokaryotic cells the oxidation and isomerisation steps proceed exclusively in extracytoplasmic environments (the lumen of the eukaryotic endoplasmic reticulum and the Gram-negative bacterial periplasmic space). The family of foldases under discussion is characterised by a conserved "thioredoxin fold" and a common active site motif: Cys-X-X-Cys. The process of disulfide bond formation relies on thiol-disulfide exchange between oxidised and reduced cysteine pairs in the catalyst and substrate protein. Two separate pathways involved in disulfide bond formation and isomerisation have been characterised both in eukaryotes and in bacteria. In the oxidative pathway, oxidizing equivalents flow from oxygen to a membrane protein (Ero1p in eukaryotes or DsbB in bacteria), and then to a folding protein containing reduced cysteines via PDI (in eukaryotes) or via DsbA (in bacteria). In the isomerisation pathway, DsbC (bacterial protein disulfide isomerase) or PDI (in eukaryotes) interacts with substrate proteins that contain non-native disulfide bonds, allowing these bonds to rearrange to their native pairings. Reducing equivalents which are necessary to maintain DsbC in a reduced form, able to attack misfolded disulfides, are transferred from the cytoplasm with the aid of the cytoplasmic membrane protein DsbD. In eukaryotes, reduced glutathione is the main source of reducing equivalents for PDI. A dual role of PDI as an oxidase and an isomerase is facilitated by its complex domain architecture.
Product Identifiers
Publisher
NOVA Science Publishers, Incorporated
ISBN-10
1606924664
ISBN-13
9781606924662
eBay Product ID (ePID)
120066200
Product Key Features
Book Title
Foldases Catalyzing the Formation and Isomerization of Disulfide Bonds in Proteins
Format
Trade Paperback
Language
English
Topic
Life Sciences / Biochemistry, Chemistry / Organic, Chemistry / General
Publication Year
2009
Genre
Science
Number of Pages
75 Pages
Dimensions
Item Length
5.5in
Item Width
8.5in
Item Weight
5.7 Oz
Additional Product Features
Lc Classification Number
Qp616.P76n337 2009
Table of Content
Preface; Introduction; Eukaryotic Protein Disulfide Isomerase (PDI); The Role of Protein Disulfide Isomerase in the Endoplasmic Reticulum; Modular Organization of the PDI Molecule and the Role of Different Domains; Functional Properties of PDI Active CentersThe pKa Values of Essential Cysteine Residues; Disulfide Isomerization: The Essential Function of PDI; The Most Significant Cellular Function of PDI Is the Isomerization of Non-Native Disulfide Bonds; The Mechanism of the Isomerization Reaction Catalyzed by PDI Depends on the Structure of Protein Substrate; Relationship between the Overall Structure of PDI Molecule and Its Activity as a Protein Disulfide Isomerase; Is PDI Capable of Discriminating between Native and Non-Native Disulfides?; Dithiol Oxidation Catalyzed by PDI; Ero1p: An Enzyme Producing Disulfide Bonds for Oxidative Protein Folding in the Endoplasmic Reticulum; The Evidence that Oxidizing Equivalents Flow from Ero1p to Substrate Proteins via PDI; The Mechanism of Ero1p Oxidative Activity in Protein Disulfide Bond Formation; The X-Ray Crystal Structure of Ero1p Reveals the Spatial Relationship between Functional Cysteines and the Bound FAD; Two Catalytic Centers of PDI Are Not Equivalent; The Role of Glutathione in Oxidative Protein Folding in Endoplasmic Reticulum; Oxidized Glutathione Does Not Provide the Oxidation Equivalents Necessary for the Formation of Disulfide Bonds; GSH Imported into the Endoplasmic Reticulum from Cytosol Can Directly Reduce PDI; Disulfide Bond Formation and Isomerization in Prokaryotes; A Pathway for Disulfide Bond Formation in the Periplasm; DsbA, a Catalyst in Disulfide Bond Formation; DsbB, a Protein Responsible for Reoxidation of DsbA; Similarities in Prokaryotic and Eukaryotic Disulfide Bond-Forming Pathways; A Pathway for Disulfide Bond Isomerization in the Periplasm; DsbC, a Disulfide Isomerase; Dimerization of DsbC Is a Prerequisite for Its Isomerase Activity; Dimerization of DsbC Protects Its Active Sites from Oxidation by DsbB; DsbG, a Paralogue of DsbC; DsbD, a Recycler of Reduced DsbC and DsbG; How Does DsbD Work?; Conclusion; Index.
Copyright Date
2009
Lccn
2009-499120
Dewey Decimal
572/.633
Dewey Edition
22
Illustrated
Yes
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- GB 864 1548 11
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