Literature DB >> 1567377

The stereochemical course of reactions catalysed by the cellobiohydrolases produced by Talaromyces emersonii.

M M Brooks1, M G Tuohy, A V Savage, M Claeyssens, M P Coughlan.   

Abstract

Three forms of exocellobiohydrolase (EC 3.2.1.91), CBH IA, CBH IB and CBH II, were isolated to apparent homogeneity from culture filtrates of the aerobic fungus Talaromyces emersonii. CBH IA and CBH II appear to be native forms of these enzymes, while CBH IB may represent a proteolytic degradation product of the CBH IA enzyme. The hydrolysis of beta-cellobiosyl fluoride by each form was monitored by 1H-n.m.r. spectroscopy. The reactions catalysed by CBH IA and CBH IB proceed with retention of the anomeric configuration, whereas that catalysed by CBH II is one of inversion. Thus one may deduce that CBH IA (or CBH IB) and CBH II operate double and single displacement reactions respectively during catalysis of substrate. On the basis of these findings and the observed substrate specificities of the various forms, one may conclude that CBH IA (and CBH IB) is a family C enzyme, while CBH II belongs to family B [Henrissat, Claeyssens, Tomme, Lemesle & Mornon (1989) Gene 81, 83-95].

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Year:  1992        PMID: 1567377      PMCID: PMC1130987          DOI: 10.1042/bj2830031

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  13 in total

1.  Direct 1H n.m.r. determination of the stereochemical course of hydrolyses catalysed by glucanase components of the cellulase complex.

Authors:  S G Withers; D Dombroski; L A Berven; D G Kilburn; R C Miller; R A Warren; N R Gilkes
Journal:  Biochem Biophys Res Commun       Date:  1986-09-14       Impact factor: 3.575

2.  Protein measurement with the Folin phenol reagent.

Authors:  O H LOWRY; N J ROSEBROUGH; A L FARR; R J RANDALL
Journal:  J Biol Chem       Date:  1951-11       Impact factor: 5.157

3.  The mechanism of fungal cellulase action. Synergism between enzyme components of Penicillium pinophilum cellulase in solubilizing hydrogen bond-ordered cellulose.

Authors:  T M Wood; S I McCrae; K M Bhat
Journal:  Biochem J       Date:  1989-05-15       Impact factor: 3.857

4.  Domain structure of cellobiohydrolase II as studied by small angle X-ray scattering: close resemblance to cellobiohydrolase I.

Authors:  P M Abuja; I Pilz; M Claeyssens; P Tomme
Journal:  Biochem Biophys Res Commun       Date:  1988-10-14       Impact factor: 3.575

5.  Properties of cellulolytic enzyme systems.

Authors:  T M Wood
Journal:  Biochem Soc Trans       Date:  1985-04       Impact factor: 5.407

6.  Synergistic hydrolysis of cellulose by components of the extracellular cellulase system of Talaromyces emersonii.

Authors:  A McHale; M P Coughlan
Journal:  FEBS Lett       Date:  1980-08-11       Impact factor: 4.124

7.  Extracellular enzyme system utilized by the fungus Sporotrichum pulverulentum (Chrysosporium lignorum) for the breakdown of cullulose. Functional characterization of five endo-1,4-beta-glucanases and one exo-1,4-beta-glucanase.

Authors:  M Streamer; K E Eriksson; B Pettersson
Journal:  Eur J Biochem       Date:  1975-11-15

8.  Cellulase families revealed by hydrophobic cluster analysis.

Authors:  B Henrissat; M Claeyssens; P Tomme; L Lemesle; J P Mornon
Journal:  Gene       Date:  1989-09-01       Impact factor: 3.688

9.  Stereochemical course of hydrolysis and hydration reactions catalysed by cellobiohydrolases I and II from Trichoderma reesei.

Authors:  M Claeyssens; P Tomme; C F Brewer; E J Hehre
Journal:  FEBS Lett       Date:  1990-04-09       Impact factor: 4.124

10.  Precise excision of the cellulose binding domains from two Cellulomonas fimi cellulases by a homologous protease and the effect on catalysis.

Authors:  N R Gilkes; R A Warren; R C Miller; D G Kilburn
Journal:  J Biol Chem       Date:  1988-07-25       Impact factor: 5.157

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  2 in total

1.  Xylose reductase from the thermophilic fungus Talaromyces emersonii: cloning and heterologous expression of the native gene (Texr) and a double mutant (TexrK271R + N273D) with altered coenzyme specificity.

Authors:  Sara Fernandes; Maria G Tuohy; Patrick G Murray
Journal:  J Biosci       Date:  2009-12       Impact factor: 1.826

2.  Stereochemical course and structure of the products of the enzymic action of endo-1,3-1,4-beta-D-glucan 4-glucanohydrolase from Bacillus licheniformis.

Authors:  C Malet; J Jiménez-Barbero; M Bernabé; C Brosa; A Planas
Journal:  Biochem J       Date:  1993-12-15       Impact factor: 3.857

  2 in total

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