Difference between revisions of "Part:BBa K1420002"

Revision as of 00:18, 10 October 2014

merB, Organomercurial Lyase from Serratia marcescens

Function

The merB gene is often found immediately downstream of merA, and is essential for the detoxification and bioremediation of organic toxic mercury compounds in congruence with merA. The merB protein is a lyase that catalyzes the breaking of carbon-mercury bonds through protonolysis of toxic mercury compounds, such as methylmercury. This produces the less toxic and less mobile Hg²⁺ which is then completely volatilized to Hg⁰ when acted upon the enzyme merA.

Structure and Mechanism

Mechanism

Enzyme MerB forms a dimer by a 2-fold pseudosymmetry around the depicted rotation axis in Figure 1. The two subunits are color coded from blue to green distinguishing the amino-terminal end of the protein from the carboxy-terminal, respectively. Active site residues are color coded as well using van der Waals sphere representation: residues Cys-96 and Cys-159 are in yellow, and residue Asp-99 is in red. Experimental Results Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
INCOMPATIBLE WITH RFC[25]
Illegal NgoMIV site found at 415
1000
COMPATIBLE WITH RFC[1000]

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 <b>Mechanism</b>
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 <p>Enzyme MerB forms a dimer by a 2-fold pseudosymmetry around the depicted rotation axis in Figure 1. The two subunits are color coded from blue to green distinguishing the amino-terminal end of the protein from the carboxy-terminal, respectively. Active site residues are color coded as well using van der Waals sphere representation: residues Cys-96 and Cys-159 are in yellow, and residue Asp-99 is in red.