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Molecular analysis of the major cellulase (CelV) of Erwinia carotovora: evidence for an evolutionary "mix-and-match" of enzyme domains.
Mol Gen Genet. 1993 Nov; 241(3-4):341-50.MG

Abstract

The structural gene for the major cellulase of Erwinia carotovora subspecies carotovora (Ecc) was isolated and expressed in Escherichia coli. Sequencing of the gene (celV) revealed a typical signal sequence and two functional domains in the enzyme; a catalytic domain linked by a short proline/threonine-rich linker to a cellulose-binding domain (CBD). The deduced amino acid sequence of the catalytic domain showed homology with cellulases of Family A, including enzymes from Bacillus spp. and Erwinia chrysanthemi CelZ, whereas the CBD showed homology with cellulases from several diverse families, supporting a "mix-and-match" hypothesis for evolution of this domain. Analysis of the substrate specificity of CelV showed it to be an endoglucanase with some exoglucanase activity. The pH optimum is about 7.0 and the temperature optimum about 42 degrees C. CelV is secreted by Ecc and by the taxonomically related Erwinia carotovora subspecies atroseptica (Eca) but not by E. coli. Overproduction of the enzyme from multicopy plasmids in Ecc appears to overload the secretory mechanism.

Authors+Show Affiliations

Department of Biological Sciences, University of Warwick, Coventry, UK.No affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

8246888

Citation

Cooper, V J., and G P. Salmond. "Molecular Analysis of the Major Cellulase (CelV) of Erwinia Carotovora: Evidence for an Evolutionary "mix-and-match" of Enzyme Domains." Molecular & General Genetics : MGG, vol. 241, no. 3-4, 1993, pp. 341-50.
Cooper VJ, Salmond GP. Molecular analysis of the major cellulase (CelV) of Erwinia carotovora: evidence for an evolutionary "mix-and-match" of enzyme domains. Mol Gen Genet. 1993;241(3-4):341-50.
Cooper, V. J., & Salmond, G. P. (1993). Molecular analysis of the major cellulase (CelV) of Erwinia carotovora: evidence for an evolutionary "mix-and-match" of enzyme domains. Molecular & General Genetics : MGG, 241(3-4), 341-50.
Cooper VJ, Salmond GP. Molecular Analysis of the Major Cellulase (CelV) of Erwinia Carotovora: Evidence for an Evolutionary "mix-and-match" of Enzyme Domains. Mol Gen Genet. 1993;241(3-4):341-50. PubMed PMID: 8246888.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Molecular analysis of the major cellulase (CelV) of Erwinia carotovora: evidence for an evolutionary "mix-and-match" of enzyme domains. AU - Cooper,V J, AU - Salmond,G P, PY - 1993/11/1/pubmed PY - 1993/11/1/medline PY - 1993/11/1/entrez SP - 341 EP - 50 JF - Molecular & general genetics : MGG JO - Mol Gen Genet VL - 241 IS - 3-4 N2 - The structural gene for the major cellulase of Erwinia carotovora subspecies carotovora (Ecc) was isolated and expressed in Escherichia coli. Sequencing of the gene (celV) revealed a typical signal sequence and two functional domains in the enzyme; a catalytic domain linked by a short proline/threonine-rich linker to a cellulose-binding domain (CBD). The deduced amino acid sequence of the catalytic domain showed homology with cellulases of Family A, including enzymes from Bacillus spp. and Erwinia chrysanthemi CelZ, whereas the CBD showed homology with cellulases from several diverse families, supporting a "mix-and-match" hypothesis for evolution of this domain. Analysis of the substrate specificity of CelV showed it to be an endoglucanase with some exoglucanase activity. The pH optimum is about 7.0 and the temperature optimum about 42 degrees C. CelV is secreted by Ecc and by the taxonomically related Erwinia carotovora subspecies atroseptica (Eca) but not by E. coli. Overproduction of the enzyme from multicopy plasmids in Ecc appears to overload the secretory mechanism. SN - 0026-8925 UR - https://www.unboundmedicine.com/medline/citation/8246888/Molecular_analysis_of_the_major_cellulase__CelV__of_Erwinia_carotovora:_evidence_for_an_evolutionary_"mix_and_match"_of_enzyme_domains_ L2 - https://doi.org/10.1007/BF00284687 DB - PRIME DP - Unbound Medicine ER -