Difference between revisions of "Part:BBa K2960007"
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MlrB is the second enzyme in the microcystin-degradation pathway. MlrB is a serine protease that catalyzes the hydrolysis of linearized MCs via the cutting of the peptide bond between alanine at position 1 and a variable amino acid (e.g. leucine) residue at position 2. This results in the formation of a tetrapeptide that is subsequently degraded by MlrC. | MlrB is the second enzyme in the microcystin-degradation pathway. MlrB is a serine protease that catalyzes the hydrolysis of linearized MCs via the cutting of the peptide bond between alanine at position 1 and a variable amino acid (e.g. leucine) residue at position 2. This results in the formation of a tetrapeptide that is subsequently degraded by MlrC. | ||
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| + | Figure 1. Schematic of the sequential degradation of MC-LR by the mlr enzyme cluster. | ||
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Revision as of 00:41, 21 October 2019
The mlrB serine protease
A cassette of enzymes endogenous to Sphingopyxis sp. has been shown to sequentially break down microcystin-LR (the most common and toxic microcystin that results from harmful algal blooms). The enzymes have been named mlrA, mlrB, mlrC, mlrD, mlrE, and mlrF.
MlrB is the second enzyme in the microcystin-degradation pathway. MlrB is a serine protease that catalyzes the hydrolysis of linearized MCs via the cutting of the peptide bond between alanine at position 1 and a variable amino acid (e.g. leucine) residue at position 2. This results in the formation of a tetrapeptide that is subsequently degraded by MlrC.
Figure 1. Schematic of the sequential degradation of MC-LR by the mlr enzyme cluster.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 1568
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI.rc site found at 1124