Difference between revisions of "Part:BBa K5117004"
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<partinfo>BBa_K5117004 short</partinfo> | <partinfo>BBa_K5117004 short</partinfo> | ||
| − | celG gene of Acetivibrio thermocellus | + | This part contains the <i>celG</i> gene of <i>Acetivibrio thermocellus</i> (synonym <i>Chlostridium thermocellum</i>) including its native signal peptide for secretion, encoding an endoglucanase (EC 3.2.1.4). |
<!-- Add more about the biology of this part here <!-- --> | <!-- Add more about the biology of this part here <!-- --> | ||
===Usage and Biology=== | ===Usage and Biology=== | ||
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| + | <span class='h3bb'>Sequence and Features</span> | ||
| + | <partinfo>BBa_K5117004 SequenceAndFeatures</partinfo> | ||
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===Enzyme characterization according to literature=== | ===Enzyme characterization according to literature=== | ||
In the study by Lemaire and Béguin (1993), titled "Nucleotide sequence of the <i>celG</i> gene of <i>Clostridium thermocellum</i> and characterization of its product, endoglucanase CelG", the researchers determined the nucleotide sequence of the <i>celG</i> gene from <i>Clostridium thermocellum</i>. This gene encodes the enzyme endoglucanase CelG, which is involved in the degradation of cellulose (Lemaire & Béguin 1993). | In the study by Lemaire and Béguin (1993), titled "Nucleotide sequence of the <i>celG</i> gene of <i>Clostridium thermocellum</i> and characterization of its product, endoglucanase CelG", the researchers determined the nucleotide sequence of the <i>celG</i> gene from <i>Clostridium thermocellum</i>. This gene encodes the enzyme endoglucanase CelG, which is involved in the degradation of cellulose (Lemaire & Béguin 1993). | ||
| + | |||
The <i>celG</i> gene spans 1,698 base pairs, encoding a polypeptide of 566 amino acids with a molecular weight of approximately 63.1 kDa (Lemaire & Béguin 1993). | The <i>celG</i> gene spans 1,698 base pairs, encoding a polypeptide of 566 amino acids with a molecular weight of approximately 63.1 kDa (Lemaire & Béguin 1993). | ||
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The enzyme acts as a typical endoglucanase, causing a significant decrease in the viscosity of Carboxymethylcellulose (CMC) solutions while releasing a relatively low amount of reducing sugars. This suggests that CelG randomly cleaves internal β-1,4-glycosidic bonds in cellulose chains. CelG exhibits activity toward substrates such as carboxy-methyl p-nitrophenyl cellulose (CNPS) and p-nitrophenyl β-D-cellobioside (PNPC). The Michaelis constant for CNPC was found to be twice that for PNPC, while the maximum velocity was 40 times higher for CNPC, indicating a higher catalytic efficiency with CNPC (data not shown in publication) (Lemaire & Béguin 1993). | The enzyme acts as a typical endoglucanase, causing a significant decrease in the viscosity of Carboxymethylcellulose (CMC) solutions while releasing a relatively low amount of reducing sugars. This suggests that CelG randomly cleaves internal β-1,4-glycosidic bonds in cellulose chains. CelG exhibits activity toward substrates such as carboxy-methyl p-nitrophenyl cellulose (CNPS) and p-nitrophenyl β-D-cellobioside (PNPC). The Michaelis constant for CNPC was found to be twice that for PNPC, while the maximum velocity was 40 times higher for CNPC, indicating a higher catalytic efficiency with CNPC (data not shown in publication) (Lemaire & Béguin 1993). | ||
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The enzyme exhibits optimal activity at a pH of 5.5 when assayed with CNPC, aligning with the acidic environments where cellulose degradation often occurs. CelG demonstrates considerable thermal stability. Less than 10% inactivation after 2 hours of incubation at 60 °C (data not shown in publication) (Lemaire & Béguin 1993). | The enzyme exhibits optimal activity at a pH of 5.5 when assayed with CNPC, aligning with the acidic environments where cellulose degradation often occurs. CelG demonstrates considerable thermal stability. Less than 10% inactivation after 2 hours of incubation at 60 °C (data not shown in publication) (Lemaire & Béguin 1993). | ||
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Its ability to degrade cellulose efficiently at elevated temperatures and acidic pH makes it a valuable enzyme for industrial applications (Lemaire & Béguin 1993). | Its ability to degrade cellulose efficiently at elevated temperatures and acidic pH makes it a valuable enzyme for industrial applications (Lemaire & Béguin 1993). | ||
| − | + | <b>More information related to this part can be found in the following publications and databases:</b> | |
| − | + | <ul> | |
| + | <li>Gene sequence: https://www.ncbi.nlm.nih.gov/nuccore/X69390</li> | ||
| + | <li>Protein sequence: https://www.ncbi.nlm.nih.gov/protein/CAA49187</li> | ||
| + | <li>UniProtKB: https://www.uniprot.org/uniprotkb/Q05332/entry</li> | ||
| + | </ul> | ||
| − | + | ===References=== | |
| − | < | + | Lemaire M. & Béguin P. (1993): Nucleotide sequence of the <i>celG</i> gene of <i>Clostridium thermocellum</i> and characterization of its product, endoglucanase CelG. Journal of bacteriology 175(11), 3353-3360. https://doi.org/10.1128/jb.175.11.3353-3360.1993 |
| − | + | ||
<!-- Uncomment this to enable Functional Parameter display | <!-- Uncomment this to enable Functional Parameter display | ||
Revision as of 18:31, 29 September 2024
AtCelG
This part contains the celG gene of Acetivibrio thermocellus (synonym Chlostridium thermocellum) including its native signal peptide for secretion, encoding an endoglucanase (EC 3.2.1.4).
Usage and Biology
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 1539
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 76
- 1000COMPATIBLE WITH RFC[1000]
Enzyme characterization according to literature
In the study by Lemaire and Béguin (1993), titled "Nucleotide sequence of the celG gene of Clostridium thermocellum and characterization of its product, endoglucanase CelG", the researchers determined the nucleotide sequence of the celG gene from Clostridium thermocellum. This gene encodes the enzyme endoglucanase CelG, which is involved in the degradation of cellulose (Lemaire & Béguin 1993).
The celG gene spans 1,698 base pairs, encoding a polypeptide of 566 amino acids with a molecular weight of approximately 63.1 kDa (Lemaire & Béguin 1993).
The enzyme acts as a typical endoglucanase, causing a significant decrease in the viscosity of Carboxymethylcellulose (CMC) solutions while releasing a relatively low amount of reducing sugars. This suggests that CelG randomly cleaves internal β-1,4-glycosidic bonds in cellulose chains. CelG exhibits activity toward substrates such as carboxy-methyl p-nitrophenyl cellulose (CNPS) and p-nitrophenyl β-D-cellobioside (PNPC). The Michaelis constant for CNPC was found to be twice that for PNPC, while the maximum velocity was 40 times higher for CNPC, indicating a higher catalytic efficiency with CNPC (data not shown in publication) (Lemaire & Béguin 1993).
The enzyme exhibits optimal activity at a pH of 5.5 when assayed with CNPC, aligning with the acidic environments where cellulose degradation often occurs. CelG demonstrates considerable thermal stability. Less than 10% inactivation after 2 hours of incubation at 60 °C (data not shown in publication) (Lemaire & Béguin 1993).
Its ability to degrade cellulose efficiently at elevated temperatures and acidic pH makes it a valuable enzyme for industrial applications (Lemaire & Béguin 1993).
More information related to this part can be found in the following publications and databases:
- Gene sequence: https://www.ncbi.nlm.nih.gov/nuccore/X69390
- Protein sequence: https://www.ncbi.nlm.nih.gov/protein/CAA49187
- UniProtKB: https://www.uniprot.org/uniprotkb/Q05332/entry
References
Lemaire M. & Béguin P. (1993): Nucleotide sequence of the celG gene of Clostridium thermocellum and characterization of its product, endoglucanase CelG. Journal of bacteriology 175(11), 3353-3360. https://doi.org/10.1128/jb.175.11.3353-3360.1993