Part:BBa_K2603003
Lac TT - Laccase from Thielavia terrestris with TEV site, Trx and HisTag
Laccase from Thielavia terrestris NRRL 8126 with an TEV site and His Tag.
Usage and Biology
Laccase is a polyphenol oxidase enzyme found in many organisms, from plants and insects to fungi and microorganisms. Known as a green catalyst, helps in the cleavage of aromatic compounds and, due to its low degree of substrate specificity, this protein is effective in the oxidation of various compounds. The active site of the enzyme has a cluster of four copper atoms, which can be distinguished by spectroscopic analysis. The first atom consists of a blue copper ion (type 1), which classifies the laccases belonging to the family of the blue copper proteins. The other three atoms are divided into one of type 2 and two type 3 ions. The enzymatic effectiveness in the oxidation of phenols occurs due to the presence of this cluster in the molecule. While copper type 1 oxidizes the substrate, the other three atoms are responsible for reducing oxygen in water. In this reaction, the oxidation electron is transferred to the three copper ions, forming a trinuclear agglomerate, which transfers electrons to the terminal acceptor oxygen. Upon receiving four electrons, the oxygen has its complete reduction. A variety of studies, in which laccase was used in the degradation of more varied micropolluants in water and soil, was performed. In these, the enzyme demonstrated the potential of application in the remediation of several compounds, such as drugs, pesticides and endocrine disruptor chemicals.
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 557
- 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 557
- 21COMPATIBLE WITH RFC[21]
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 557
- 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 557
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI site found at 1258
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