Characterization of the gene celD and its encoded product 1,4-beta-D-glucan glucohydrolase D from Pseudomonas fluorescens subsp. cellulosa - PubMed (original) (raw)
Comparative Study
. 1992 Aug 1;285 ( Pt 3)(Pt 3):947-55.
doi: 10.1042/bj2850947.
Affiliations
- PMID: 1497631
- PMCID: PMC1132887
- DOI: 10.1042/bj2850947
Comparative Study
Characterization of the gene celD and its encoded product 1,4-beta-D-glucan glucohydrolase D from Pseudomonas fluorescens subsp. cellulosa
J E Rixon et al. Biochem J. 1992.
Abstract
A genomic library of Pseudomonas fluorescens subsp. cellulosa DNA constructed in pUC18 and expressed in Escherichia coli was screened for recombinants expressing 4-methylumbelliferyl beta-D-glucoside hydrolysing activity (MUGase). A single MUGase-positive clone was isolated. The MUGase hydrolysed cellobiose, cellotriose, cellotetraose, cellopentaose and cellohexaose to glucose, by sequentially cleaving glucose residues from the non-reducing end of the cello-oligosaccharides. The Km values for cellobiose and cellohexaose hydrolysis were 1.2 mM and 28 microM respectively. The enzyme exhibited no activity against soluble or insoluble cellulose, xylan and xylobiose. Thus the MUGase is classified as a 1,4-beta-D-glucan glucohydrolase (EC 3.2.1.74) and is designated 1,4-beta-D-glucan glucohydrolase D (CELD). When expressed by E. coli, CELD was located in the cell-envelope fraction; a significant proportion of the native enzyme was also associated with the cell envelope when synthesized by its endogenous host. The nucleotide sequence of the gene, celD, which encodes CELD, revealed an open reading frame of 2607 bp, encoding a protein of M(r) 92,000. The deduced primary structure of CELD was confirmed by the M(r) of CELD (85,000) expressed by E. coli and P. fluorescens subsp. cellulosa, and by the experimentally determined N-terminus of the enzyme purified from E. coli, which showed identity with residues 52-67 of the celD translated sequence. The structure of the N-terminal region of full-length CELD was similar to the signal peptides of P. fluorescens subsp. cellulosa plant-cell-wall hydrolases. Deletion of the N-terminal 47 residues of CELD solubilized MUGase activity in E. coli. CELD exhibited sequence similarity with beta-glucosidase B of Clostridium thermocellum, particularly in the vicinity of the active-site aspartate residue, but did not display structural similarity with the mature forms of cellulases and xylanases expressed by P. fluorescens subsp. cellulosa.
Similar articles
- The cellodextrinase from Pseudomonas fluorescens subsp. cellulosa consists of multiple functional domains.
Ferreira LM, Hazlewood GP, Barker PJ, Gilbert HJ. Ferreira LM, et al. Biochem J. 1991 Nov 1;279 ( Pt 3)(Pt 3):793-9. doi: 10.1042/bj2790793. Biochem J. 1991. PMID: 1953673 Free PMC article. - Xylanase B and an arabinofuranosidase from Pseudomonas fluorescens subsp. cellulosa contain identical cellulose-binding domains and are encoded by adjacent genes.
Kellett LE, Poole DM, Ferreira LM, Durrant AJ, Hazlewood GP, Gilbert HJ. Kellett LE, et al. Biochem J. 1990 Dec 1;272(2):369-76. doi: 10.1042/bj2720369. Biochem J. 1990. PMID: 2125205 Free PMC article. - The non-catalytic cellulose-binding domain of a novel cellulase from Pseudomonas fluorescens subsp. cellulosa is important for the efficient hydrolysis of Avicel.
Hall J, Black GW, Ferreira LM, Millward-Sadler SJ, Ali BR, Hazlewood GP, Gilbert HJ. Hall J, et al. Biochem J. 1995 Aug 1;309 ( Pt 3)(Pt 3):749-56. doi: 10.1042/bj3090749. Biochem J. 1995. PMID: 7639689 Free PMC article. - A non-modular endo-beta-1,4-mannanase from Pseudomonas fluorescens subspecies cellulosa.
Braithwaite KL, Black GW, Hazlewood GP, Ali BR, Gilbert HJ. Braithwaite KL, et al. Biochem J. 1995 Feb 1;305 ( Pt 3)(Pt 3):1005-10. doi: 10.1042/bj3051005. Biochem J. 1995. PMID: 7848261 Free PMC article. - Structure and function analysis of Pseudomonas plant cell wall hydrolases.
Hazlewood GP, Gilbert HJ. Hazlewood GP, et al. Prog Nucleic Acid Res Mol Biol. 1998;61:211-41. doi: 10.1016/s0079-6603(08)60828-4. Prog Nucleic Acid Res Mol Biol. 1998. PMID: 9752722 Review.
Cited by
- Comprehensive functional characterization of the glycoside hydrolase family 3 enzymes from Cellvibrio japonicus reveals unique metabolic roles in biomass saccharification.
Nelson CE, Attia MA, Rogowski A, Morland C, Brumer H, Gardner JG. Nelson CE, et al. Environ Microbiol. 2017 Dec;19(12):5025-5039. doi: 10.1111/1462-2920.13959. Epub 2017 Dec 7. Environ Microbiol. 2017. PMID: 29052930 Free PMC article. - Systems analysis in Cellvibrio japonicus resolves predicted redundancy of β-glucosidases and determines essential physiological functions.
Nelson CE, Rogowski A, Morland C, Wilhide JA, Gilbert HJ, Gardner JG. Nelson CE, et al. Mol Microbiol. 2017 Apr;104(2):294-305. doi: 10.1111/mmi.13625. Epub 2017 Feb 28. Mol Microbiol. 2017. PMID: 28118504 Free PMC article. - Polysaccharide degradation systems of the saprophytic bacterium Cellvibrio japonicus.
Gardner JG. Gardner JG. World J Microbiol Biotechnol. 2016 Jul;32(7):121. doi: 10.1007/s11274-016-2068-6. Epub 2016 Jun 4. World J Microbiol Biotechnol. 2016. PMID: 27263016 Review. - Carbohydrate-active enzymes identified by metagenomic analysis of deep-sea sediment bacteria.
Klippel B, Sahm K, Basner A, Wiebusch S, John P, Lorenz U, Peters A, Abe F, Takahashi K, Kaiser O, Goesmann A, Jaenicke S, Grote R, Horikoshi K, Antranikian G. Klippel B, et al. Extremophiles. 2014 Sep;18(5):853-63. doi: 10.1007/s00792-014-0676-3. Epub 2014 Aug 10. Extremophiles. 2014. PMID: 25108363 - Synthesis of three advanced biofuels from ionic liquid-pretreated switchgrass using engineered Escherichia coli.
Bokinsky G, Peralta-Yahya PP, George A, Holmes BM, Steen EJ, Dietrich J, Lee TS, Tullman-Ercek D, Voigt CA, Simmons BA, Keasling JD. Bokinsky G, et al. Proc Natl Acad Sci U S A. 2011 Dec 13;108(50):19949-54. doi: 10.1073/pnas.1106958108. Epub 2011 Nov 28. Proc Natl Acad Sci U S A. 2011. PMID: 22123987 Free PMC article.
References
- Mol Gen Genet. 1989 May;217(1):70-6 - PubMed
- J Gen Microbiol. 1990 Oct;136(10):2089-97 - PubMed
- Gene. 1989 Sep 1;81(1):83-95 - PubMed
- J Bacteriol. 1988 Jan;170(1):301-7 - PubMed
- Curr Genet. 1987;12(3):175-84 - PubMed
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources