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PMID:12200312
| Citation |
Saloheimo, M, Kuja-Panula, J, Ylösmäki, E, Ward, M and Penttilä, M (2002) Enzymatic properties and intracellular localization of the novel Trichoderma reesei beta-glucosidase BGLII (cel1A). Appl. Environ. Microbiol. 68:4546-53 |
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| Abstract |
This paper describes the characterization of an intracellular beta-glucosidase enzyme BGLII (Cel1a) and its gene (bgl2) from the cellulolytic fungus Trichoderma reesei (Hypocrea jecorina). The expression pattern of bgl2 is similar to that of other cellulase genes known from this fungus, and the gene would appear to be under the control of carbon catabolite repression mediated by the cre1 gene. The BGLII protein was produced in Escherichia coli, and its enzymatic properties were analyzed. It was shown to be a specific beta-glucosidase, having no beta-galactosidase side activity. It hydrolyzed both cellotriose and cellotetraose. BGLII exhibited transglycosylation activity, producing mainly cellotriose from cellobiose and sophorose and cellobiose from glucose. Antibodies raised against BGLII showed the presence of the enzyme in T. reesei cell lysates but not in the culture supernatant. Activity measurements and Western blot analysis of T. reesei strains expressing bgl2 from a constitutive promoter further confirmed the intracellular localization of this beta-glucosidase. |
| Links | |
| Keywords |
Gene Expression; Glucan Endo-1,3-beta-D-Glucosidase/genetics; Glucan Endo-1,3-beta-D-Glucosidase/isolation & purification; Glucan Endo-1,3-beta-D-Glucosidase/metabolism; Glycosylation; Hydrolysis; Sequence Homology, Amino Acid; Trichoderma/enzymology; Trichoderma/genetics |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0005737: cytoplasm |
ECO:0000314: |
C |
FIG 4,5. This would suggest that BGLII is not bound to the cell wall and resides neither in the periplasmic space nor at the plasma membrane, since PNP-beta-D-glucoside, which was used as a substrate, most probably can diffuse through the cell wall. Thus, it is very likely that BGLII is a cytoplasmic protein. This is also consistent with the pH profile of BGLII. Unlike the secreted T. reesei cellulases that have acidic pH optima, BGLII is most active at levels of pH close to neutral. |
complete | ||||
| GO:0031217 : glucan 1,4-beta-glucosidase activity |
ECO:0000314: |
F |
Table 1 |
complete | ||||
| GO:0016758: transferase activity, transferring hexosyl groups |
ECO:0000314: |
F |
Fig 3 |
complete | ||||
|
enables |
GO:0008422: beta-glucosidase activity |
ECO:0000314: direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
| GO:0008422: beta-glucosidase activity |
ECO:0000314: |
F |
Table 2. |
complete | ||||
|
enables |
GO:0008422: beta-glucosidase activity |
ECO:0000314: direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
See also
References
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