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Query: UNIPROT:P06889 (Mol)
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Endoglucanase C (CenC) from Cellulomonas fimi binds to cellulose and to Sephadex. The enzyme has two contiguous 150-amino-acid repeats (N1 and N2) at its N-terminus and two unrelated contiguous 100-amino-acid repeats (C1 and C2) at its C-terminus. Polypeptides corresponding to N1, N1N2, C1, and C1C2 were produced by expression of appropriate cenC gene fragments in Escherichia coli. N1N2, but not N1 alone, binds to Sephadex; both polypeptides bind to Avicel, (a heterogeneous cellulose preparation containing both crystalline and non-crystalline components). Neither C1 nor C1C2 binds to Avicel or Sephadex. N1N2 and N1 bind to regenerated ('amorphous') cellulose but not to bacterial crystalline cellulose; the cellulose-binding domain of C. fimi exoglucanase Cex binds to both of these forms of cellulose. Amino acid sequence comparison reveals that N1 and N2 are distantly related to the cellulose-binding domains of Cex and C. fimi endoglucanases A and B.
Mol Microbiol 1992 May
PMID:The binding of Cellulomonas fimi endoglucanase C (CenC) to cellulose and Sephadex is mediated by the N-terminal repeats. 137 11

The nucleotide sequence of engD, an endo-beta-1,4-glucanase gene from Clostridium cellulovorans was determined (Genbank Accession No. M37434). The COOH-terminal part of the gene product, EngD, contained a Thr-Thr-Pro repeated sequence followed by a region that has homology to the exoglucanase of Cellulomonas fimi. EngD and EngB, another C. cellulovorans endoglucanase, show 75% amino acid sequence homology at their NH2-termini, in contrast to their carboxyterminal domains which show no homology. EngD had endoglucanase activity on carboxymethylcellulose (CMC), cellobiosidase activity on p-nitrophenyl-cellobioside (p-NPC), and partial hydrolytic activity on crystalline cellulose (Avicel), while EngB showed hydrolytic activity against only CMC. Chimeric proteins between EngB and EngD were constructed by exchanging the non-homologous COOH-terminal regions. Chimeric proteins that contained the NH2-terminus of EngD retained cellobiosidase activity but chimeras with the EngB NH2-terminus showed no cellobiosidase activity. Hydrolysis of crystalline cellulose (Avicelase activity) was observed only with the enzyme containing the EngD NH2-terminus and EngD COOH-terminus.
Mol Gen Genet 1992 Feb
PMID:Analysis of functional domains of endoglucanases from Clostridium cellulovorans by gene cloning, nucleotide sequencing and chimeric protein construction. 153

An exoglucanase, with specificity for beta (1,3) linkages, from the cell wall of Candida albicans has been crystallized by the hanging drop method in the presence of polyethylene glycol 8000. The crystals, which diffract to better than 1.9 A resolution, belong to the orthorhombic space group P212121 with cell constants a = 60.2 A, b = 65.2 A, c = 96.5 A and with one molecule in the asymmetric unit.
J Mol Biol 1992 May 05
PMID:Crystallization of the exo(1,3)-beta-glucanase from Candida albicans. 158 91

The cloning, expression and nucleotide sequence of a 3 kb DNA segment on pLS206 containing a xylanase gene (xynB) from Butyrivibrio fibrisolvens H17c was investigated. The open reading frame (ORF) of 1905 bp encoded a xylanase of 635 amino acid residues (Mr 73156). At least 850 bp at the 3' end of the gene could be deleted without loss of xylanase activity. The deduced amino acid sequence was confirmed by purifying the enzyme and subjecting it to N-terminal amino acid sequence analysis. In Escherichia coli C600 (pLS206) cells the xylanase was localized in the cytoplasm. Its optimum pH for activity was between pH 5.4 and 6, and optimum temperature 55 degrees C. The primary structure of the xylanase showed a significant level of identity with a cellobiohydrolase/endoglucanase of Caldocellum saccharolyticum, as well as with the xylanases of the alkaliphilic Bacillus sp. strain C-125, B. fibrisolvens strain 49, and Pseudomonas fluorescens subsp. cellulosa.
Mol Gen Genet 1991 Aug
PMID:Cloning, sequencing and expression of a gene encoding a 73 kDa xylanase enzyme from the rumen anaerobe Butyrivibrio fibrisolvens H17c. 190 24

The nucleotide sequence of a 2.8 kb DNA segment containing an endoglucanase gene (end1) from Butyrivibrio fibrisolvens H17c was determined. The B. fibrisolvens H17c gene was expressed from its own regulatory region in Escherichia coli and three putative consensus promoter sequences were identified upstream of a ribosome binding site and an ATG start codon. The complete amino acid sequence (547 residues) was deduced and homology with the Clostridium thermocellum celE gene product (EGE) was demonstrated. The endoglucanase contained a typical amino-terminal signal sequence and five repeated sequences (PDPTPVD) between amino acids 412-447. The endoglucanase showed relatively high endoglucanase activity against endoglucanase-specific substrates with beta 1-4 linkages but low activity against xylan and an exoglucanase-specific substrate, p-nitrophenyl-beta-D-cellobioside.
Mol Gen Genet 1989 Oct
PMID:Cloning and sequencing of an endoglucanase (end1) gene from Butyrivibrio fibrisolvens H17c. 261 59

Single crystals of the core protein of the cellulase cellobiohydrolase II have been grown in polyethylene glycol 6000 with the hanging drop method. Successful crystallization occurred only when 82 amino acids were removed from the N terminus by papain cleavage. Crystals belong to the space group P2(1) and have cell constants a = 49.1 A, b = 75.8 A, c = 92.9 A, beta = 103.2. The diffraction pattern extends to better than 2.0 A.
J Mol Biol 1989 Sep 05
PMID:Crystallization of the core protein of cellobiohydrolase II from Trichoderma reesei. 281 Mar 67

A genomic library of Pseudomonas fluorescens subsp. cellulosa DNA was constructed in bacteriophage lambda 47.1 and recombinants expressing carboxymethylcellulase (CMCase) activity isolated. A 7.3 kb partial EcoRI fragment, a 9.4 kb EcoRI fragment and a 5.8 kb HindIII fragment were subcloned from three different phages into pUC18 to yield recombinant plasmids pJHH1, pJHH3 and pGJH2 respectively. Cells of Escherichia coli harbouring these plasmids expressed CMCase activity. The positions of the CMCase genes in the three plasmids were determined by subcloning and transposon mutagenesis. pJHH1 contained two distinct DNA regions encoding CMCases, which were controlled by the same promoter. All four cloned enzymes cleaved p-nitrophenyl-beta-D-glucopyranoside, although at a very low rate, but none exhibited exoglucanase activity. In common with other extracellular enzymes cloned in E. coli, all the CMCases were exported to the periplasmic space in the enteric bacterium. The carboxymethylcellulase genes encoded by pJHH1 and pJHH3, were subject to glucose repression in E. coli.
Mol Gen Genet 1987 Dec
PMID:Evidence for multiple carboxymethylcellulase genes in Pseudomonas fluorescens subsp. cellulosa. 332 49

We have investigated the effect of disruption of the bgl1-(beta-glucosidase l-encoding) gene of Trichoderma reesei on the formation of other beta-glucosidase activities and on the induction of cellulases. To this end the bgl1 locus was disrupted by insertion of the Aspergillus nidulans amdS (acetamidase-encoding) gene. The bgl1-disrupted strain did not produce the 75 kDa extracellular beta-glucosidase on cellulose or lactose, but still formed beta-glucosidase activity on glucose, cellobiose, xylan or beta-1,3-glucan, suggesting that the enzyme(s) exhibiting this beta-glucosidase activity is (are) not encoded by bgl1. The cellulase-inducer sophorose induced the bgl1-encoded beta-glucosidase, whereas the remaining beta-glucosidase activity was induced by methyl-beta-D-glucoside. The bgl1-gene product was mainly secreted into the medium, whereas the other beta-glucosidase activity was mainly associated with the cells. A bgl1-multicopy strain formed higher amounts of cellulases than the parent strain. Nonsaturating concentrations of sophorose efficiently induced cellobiohydrolase l formation in the bgl1-multicopy strain, but less efficiently in the bgl1-disrupted strain. The multicopy strain and the parent strain were comparably efficient at saturating sophorose concentrations. The beta-glucosidase inhibitor nojirimycin strongly inhibited induction in all strains. These data suggest that the bgl1-encoded beta-glucosidase is not identical to the plasma-membrane-bound, constitutive, methyl-beta-glucoside inducible beta-glucosidase, but represents an extracellular cellulose-induced enzyme. Both enzymes contribute to rapid induction of cellulases by modifying the inducer sophorose.
Mol Microbiol 1995 May
PMID:The bgl1 gene of Trichoderma reesei QM 9414 encodes an extracellular, cellulose-inducible beta-glucosidase involved in cellulase induction by sophorose. 747 63

An endoglucanase (EG5) of Clostridium thermocellum was purified to the homogeneity from the recombinant strains of Escherichia coli. The elution pattern of EG5 on gel filtration column showed the Mr of 100 kDa. However, the SDS-PAGE of the same protein showed the Mr of 35 kDa. This indicates the formation of a soluble trimeric complex by EG5 in non-denaturing conditions. The complex was found to be stable in 100 mM Na-taurocholate or 0.1% (w/v) Nonidet P-40. The hydrophilic nature of EG5 was confirmed by its unretarded elution at high salt concentrations from gel filtration columns. pI of EG5 was determined as 4.75. The EG5 was shown to possess high thermostability (stable at 65 degrees C for several days) and a broad pH range of activity from 5.5 to 7.5. The EG5 was capable of degrading a variety of soluble cellulosic substrates, and was able to enhance the rate and extent of soluble and natural crystalline cellulose hydrolysis by a cellobiohydrolase (CBH3) of C. thermocellum. The combination of properties, like intramolecular complex formation, high thermostability and positive synergistic effect offered by a cellulolytic component of C. thermocellum is being reported for the first time.
Biochem Mol Biol Int 1994 Mar
PMID:Isolation and characterization of a complex forming hydrophilic endoglucanase of Clostridium thermocellum. 803 10

The genome of Phanerochaete chrysosporium strain ME446 contains multiple, non-allelic, cellobiohydrolase I (CBHI)-like sequences, at least two of which are expressed in a cellulose-dependent manner. Each of the expressed genes contains two identically positioned introns within its coding region. The lengths and sequences of these introns are different and one is not excised from all transcripts, raising the possibility that subtly different protein products may be expressed from a common gene. Introns are also present upstream of both genes but these differ in number and position, as well as sequence and length. Endoglucanase-like sequences could not be identified and it is suggested that variant CBHI-like proteins may provide endoglucanase activity in this fungus.
Mol Microbiol 1994 Apr
PMID:Differential expression of multiple exo-cellobiohydrolase I-like genes in the lignin-degrading fungus Phanerochaete chrysosporium. 805 46


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