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Activity enhancement of Cel5Z from Pectobacterium chrysanthemi PY35 by removing C-terminal region.
Biochem Biophys Res Commun. 2002 Feb 22; 291(2):425-30.BB

Abstract

The phytopathogenic bacterium Pectobacteium chrysanthemi PY35 secretes Cel5Z endoglucanase belonging to the glycoside hydrolase family 5 of EC 3.2.1.4. The mutation of cel5Z::Omega gene was constructed by cloning the 2.0-kb SmaI fragment containing the streptomycin/spectinomycin-resistance gene of pHP45(Omega) into the BalI site of pPY100. The insertion of Omega fragment generated a new stop codon, removing the Ser/Thr-rich linker region and the cellulose binding domain (CBD) in the C-terminal region of cel5Z gene. By subsequent subcloning from this 4.9-kb fragment (pPY1001), a 1.0-kb (pPY1002) fragment was obtained and designated as cel5Z::Omega. The cel5Z::Omega gene had an open reading frame (ORF) of 1011 bp, encoding 336 amino acids, starting with an ATG codon and ending with a new TGA stop codon. The molecular mass of the Cel5Z::Omega protein in E. coli transformant appeared to be 32 kDa by SDS-PAGE analysis in the presence of carboxymethyl-cellulose (CMC). The Cel5Z::Omega protein hydrolyzed CMC with 1.7-fold higher activity than the intact Cel5Z cellulase.

Authors+Show Affiliations

Research Institute of Life Science, Gyeongsang National University, Chinju 660-701, Korea.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

11846423

Citation

Park, Sang Ryeol, et al. "Activity Enhancement of Cel5Z From Pectobacterium Chrysanthemi PY35 By Removing C-terminal Region." Biochemical and Biophysical Research Communications, vol. 291, no. 2, 2002, pp. 425-30.
Park SR, Cho SJ, Kim MK, et al. Activity enhancement of Cel5Z from Pectobacterium chrysanthemi PY35 by removing C-terminal region. Biochem Biophys Res Commun. 2002;291(2):425-30.
Park, S. R., Cho, S. J., Kim, M. K., Ryu, S. K., Lim, W. J., An, C. L., Hong, S. Y., Kim, J. H., Kim, H., & Yun, H. D. (2002). Activity enhancement of Cel5Z from Pectobacterium chrysanthemi PY35 by removing C-terminal region. Biochemical and Biophysical Research Communications, 291(2), 425-30.
Park SR, et al. Activity Enhancement of Cel5Z From Pectobacterium Chrysanthemi PY35 By Removing C-terminal Region. Biochem Biophys Res Commun. 2002 Feb 22;291(2):425-30. PubMed PMID: 11846423.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Activity enhancement of Cel5Z from Pectobacterium chrysanthemi PY35 by removing C-terminal region. AU - Park,Sang Ryeol, AU - Cho,Soo Jeong, AU - Kim,Min Keun, AU - Ryu,Sung Kee, AU - Lim,Woo Jin, AU - An,Chang Long, AU - Hong,Su Young, AU - Kim,Jeong Hwan, AU - Kim,Hoon, AU - Yun,Han Dae, PY - 2002/2/16/pubmed PY - 2002/3/20/medline PY - 2002/2/16/entrez SP - 425 EP - 30 JF - Biochemical and biophysical research communications JO - Biochem Biophys Res Commun VL - 291 IS - 2 N2 - The phytopathogenic bacterium Pectobacteium chrysanthemi PY35 secretes Cel5Z endoglucanase belonging to the glycoside hydrolase family 5 of EC 3.2.1.4. The mutation of cel5Z::Omega gene was constructed by cloning the 2.0-kb SmaI fragment containing the streptomycin/spectinomycin-resistance gene of pHP45(Omega) into the BalI site of pPY100. The insertion of Omega fragment generated a new stop codon, removing the Ser/Thr-rich linker region and the cellulose binding domain (CBD) in the C-terminal region of cel5Z gene. By subsequent subcloning from this 4.9-kb fragment (pPY1001), a 1.0-kb (pPY1002) fragment was obtained and designated as cel5Z::Omega. The cel5Z::Omega gene had an open reading frame (ORF) of 1011 bp, encoding 336 amino acids, starting with an ATG codon and ending with a new TGA stop codon. The molecular mass of the Cel5Z::Omega protein in E. coli transformant appeared to be 32 kDa by SDS-PAGE analysis in the presence of carboxymethyl-cellulose (CMC). The Cel5Z::Omega protein hydrolyzed CMC with 1.7-fold higher activity than the intact Cel5Z cellulase. SN - 0006-291X UR - https://www.unboundmedicine.com/medline/citation/11846423/Activity_enhancement_of_Cel5Z_from_Pectobacterium_chrysanthemi_PY35_by_removing_C_terminal_region_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006291X02964375 DB - PRIME DP - Unbound Medicine ER -