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Title: Interfacial molecular interactions of cellobiohydrolase Cel7A and its variants on cellulose

Journal Article · · Biotechnology for Biofuels
ORCiD logo [1]; ORCiD logo [2];  [3];  [4];  [1];  [5]; ORCiD logo [1]
  1. Univ. of California, Davis, CA (United States)
  2. Los Alamos National Lab. (LANL), Los Alamos, NM (United States)
  3. Gracenote, Inc., Emoryville, CA (United States)
  4. Univ. of California, Davis, CA (United States); Silpakorn Univ., Nakhon Pathom (Thailand)
  5. Univ. of California, Davis, CA (United States); Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
+ Show Author Affiliations

Molecular-scale mechanisms of the enzymatic breakdown of cellulosic biomass into fermentable sugars are still poorly understood, with a need for independent measurements of enzyme kinetic parameters. We measured binding times of cellobiohydrolase Trichoderma reesei Cel7A (Cel7A) on celluloses using wild-type Cel7A (WTintact), the catalytically deficient mutant Cel7A E212Q (E212Qintact) and their proteolytically isolated catalytic domains (CD) (WTcore and E212Qcore, respectively). The binding time distributions were obtained from time-resolved, super-resolution images of fluorescently labeled enzymes on cellulose obtained with total internal reflection fluorescence microscopy.

Research Organization:
Los Alamos National Laboratory (LANL), Los Alamos, NM (United States)
Sponsoring Organization:
USDOE Office of Science (SC). Basic Energy Sciences (BES) (SC-22)
Grant/Contract Number:
89233218CNA000001
OSTI ID:
1630858
Report Number(s):
LA-UR--19-28848
Journal Information:
Biotechnology for Biofuels, Journal Name: Biotechnology for Biofuels Journal Issue: 1 Vol. 13; ISSN 1754-6834
Publisher:
BioMed CentralCopyright Statement
Country of Publication:
United States
Language:
English

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The Mechanism of Cellulose Hydrolysis by a Two-Step, Retaining Cellobiohydrolase Elucidated by Structural and Transition Path Sampling Studies journal December 2013
The Energy Landscape for the Interaction of the Family 1 Carbohydrate-Binding Module and the Cellulose Surface is Altered by Hydrolyzed Glycosidic Bonds journal August 2009
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Processivity of Cellobiohydrolases Is Limited by the Substrate journal November 2010
Pre-steady-state Kinetics for Hydrolysis of Insoluble Cellulose by Cellobiohydrolase Cel7A journal April 2012
Binding and Movement of Individual Cel7A Cellobiohydrolases on Crystalline Cellulose Surfaces Revealed by Single-molecule Fluorescence Imaging journal July 2013
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Single-molecule Imaging Analysis of Binding, Processive Movement, and Dissociation of Cellobiohydrolase Trichoderma reesei Cel6A and Its Domains on Crystalline Cellulose journal September 2016
Inter-domain Synergism Is Required for Efficient Feeding of Cellulose Chain into Active Site of Cellobiohydrolase Cel7A journal October 2016
Characterization of structures from X-ray scattering data using genetic algorithms
  • Wormington, Matthew; Panaccione, Charles; Matney, Kevin M.
  • Philosophical Transactions of the Royal Society of London. Series A: Mathematical, Physical and Engineering Sciences, Vol. 357, Issue 1761 https://doi.org/10.1098/rsta.1999.0469
journal October 1999
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Harnessing the potential of LPMO-containing cellulase cocktails poses new demands on processing conditions journal November 2015
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Cited By (2)

Single-Molecule Image Sequences of Trichoderma reesei Cel7A and Variants on Cellulose Fibrils dataset January 2020
Single-Molecule Image Sequences of Trichoderma reesei Cel7A and Variants on Cellulose Fibrils dataset January 2020

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