Difference between revisions of "Part:BBa K5136026"
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<b>Cellulase EG5C</b> | <b>Cellulase EG5C</b> | ||
<br> | <br> | ||
+ | <b>Biology</b> | ||
+ | <br> | ||
+ | <b>Cellulase</b> | ||
+ | <br> | ||
+ | Efficient hydrolysis of cellulose to glucose depends on the synchronized action of three classes of enzymes, endoglucanase, exoglucanase and β-glucosidase. Processivity is a common mode of action for many exoglucanases and plays a key role in the complete hydrolysis of crystalline cellulose. In contrast, classic endoglucanases randomly cleave β-1,4-glycosidic bonds in the interior of the cellulosic chains and have been considered to be non-processive. Studies have shown that in contrast to other cellulolytic systems that dependent on both endo and exoglucanases, a processive endoglucanase coupled with a β-glucosidase may be sufficient for the degradation of cellulose. Cellulase EG5C is a kind of proteins found from | ||
+ | <b><i>Bacillus subtilis</I></b> | ||
+ | BS-5 (1). It is hypothesized that | ||
+ | <b><i>B. subtilis</I></b> | ||
+ | BS-5 might produce a processive endoglucanase, which might substitute for the apparent deficiency in exoglucanase activity. | ||
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Revision as of 12:42, 17 September 2024
cellulase EG5C-His tag
Cellulase EG5C
Biology
Cellulase
Efficient hydrolysis of cellulose to glucose depends on the synchronized action of three classes of enzymes, endoglucanase, exoglucanase and β-glucosidase. Processivity is a common mode of action for many exoglucanases and plays a key role in the complete hydrolysis of crystalline cellulose. In contrast, classic endoglucanases randomly cleave β-1,4-glycosidic bonds in the interior of the cellulosic chains and have been considered to be non-processive. Studies have shown that in contrast to other cellulolytic systems that dependent on both endo and exoglucanases, a processive endoglucanase coupled with a β-glucosidase may be sufficient for the degradation of cellulose. Cellulase EG5C is a kind of proteins found from
Bacillus subtilis
BS-5 (1). It is hypothesized that
B. subtilis BS-5 might produce a processive endoglucanase, which might substitute for the apparent deficiency in exoglucanase activity.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12INCOMPATIBLE WITH RFC[12]Illegal NheI site found at 958
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 610
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI site found at 620