Difference between revisions of "Part:BBa K936000"
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<partinfo>BBa_K936000 short</partinfo> | <partinfo>BBa_K936000 short</partinfo> | ||
| − | This is the LC Cutinase gene used to break PET into terephthalic acid and ethylene glycol. | + | This is the LC Cutinase gene used to break PET into terephthalic acid and ethylene glycol. The enzyme Cutinase is a lypolytic/esterolytic enzyme that degrades cutin, which is found in most plant and fungi' cuticles. They enzyme itself is more commonly found in plants and bacteria. Cutinase also can degrades water soluble esters and insoluble triglycerides. The enzyme hydrolyzes these substrates by creating an acyl enzyme intermediate. A metagenomic analysis was done in order to find more novel enzymes such as lipases, esterases, proteases, and cellulases, as well as furthering our knowledge of protein sequence space in the environment. Naturally, compost samples would have enzymes that degrade cell walls and other compounds with potentially useful applications. A novel homolog of cutinase, known as Leaf Compost Cutinase (LC) was found to have a 57.4% genetic similarity to cutinase found in ''T. Fusca'', meriting an experiment to overproduce the protein in ''E. Coli''. The study found that it's applications could be most valuable in the textile industry, among other material fields. |
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It should be noted that ethylene glycol is moderately toxic to humans and other animals. | It should be noted that ethylene glycol is moderately toxic to humans and other animals. | ||
<!-- Add more about the biology of this part here | <!-- Add more about the biology of this part here | ||
| − | + | FROM SOURCE ARTICLE: "It hydrolyzes these substrates to carboxylic acids and alcohols through the formation of an acyl enzyme intermediate, in which the active-site serine residue is acylated by the substrate. This serine residue is located within a GXSXG sequence motif and forms a catalytic triad with His and Asp." | |
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<span class='h3bb'>Sequence and Features</span> | <span class='h3bb'>Sequence and Features</span> | ||
Revision as of 00:56, 29 September 2012
LC Cutinase
This is the LC Cutinase gene used to break PET into terephthalic acid and ethylene glycol. The enzyme Cutinase is a lypolytic/esterolytic enzyme that degrades cutin, which is found in most plant and fungi' cuticles. They enzyme itself is more commonly found in plants and bacteria. Cutinase also can degrades water soluble esters and insoluble triglycerides. The enzyme hydrolyzes these substrates by creating an acyl enzyme intermediate. A metagenomic analysis was done in order to find more novel enzymes such as lipases, esterases, proteases, and cellulases, as well as furthering our knowledge of protein sequence space in the environment. Naturally, compost samples would have enzymes that degrade cell walls and other compounds with potentially useful applications. A novel homolog of cutinase, known as Leaf Compost Cutinase (LC) was found to have a 57.4% genetic similarity to cutinase found in T. Fusca, meriting an experiment to overproduce the protein in E. Coli. The study found that it's applications could be most valuable in the textile industry, among other material fields.
It should be noted that ethylene glycol is moderately toxic to humans and other animals.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 600
- 1000COMPATIBLE WITH RFC[1000]