Difference between revisions of "Part:BBa K3823001"

Revision as of 08:56, 19 October 2021

SQR(Sulfide: Quinone Oxidoreductase) from Acidithiobacillus spp.

Sulfide: quinone oxidoreductase(SQR), is an ancient flavoprotein of the disulfide oxidoreductase family that is present in nearly all domains of life. It can oxidize sulfide to zero-valent sulfur. SQRs were first found in sulfide trophic bacteria, later SQR-like enzymes were found in the mitochondria of some fungi, as well as in all animal species whose genomes have been sequenced . Several SQRs have been purified and characterized by biochemical methods. They are considered to be integral monotopic membrane proteins, associating with the membrane through amphipathic helices. The monomeric molecular mass of the enzyme is around 50 kDa. The enzyme usually harbors a covalently-bound FAD cofactor in each monomer. However, FAD can also be non-covalently bound as in the SQR of A. ferrooxidans and some other organisms.

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 42
Illegal NgoMIV site found at 466
Illegal AgeI site found at 961
1000
COMPATIBLE WITH RFC[1000]

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 <partinfo>BBa_K3823001 short</partinfo>
-Sqr can oxydize hydrogen sulfide to zero-valent sulfur.
+Sulfide: quinone oxidoreductase(SQR), is an ancient flavoprotein of the disulfide oxidoreductase family that is present in nearly all domains of life. It can oxidize sulfide  to zero-valent sulfur. SQRs were first found in sulfide trophic bacteria, later SQR-like enzymes were found in the mitochondria of some fungi, as well as in all animal species whose genomes have been sequenced . Several SQRs have been purified and characterized by biochemical methods. They are considered to be integral monotopic membrane proteins, associating with the membrane through amphipathic helices. The monomeric molecular mass of the enzyme is around 50 kDa. The enzyme usually harbors a covalently-bound FAD cofactor in each monomer. However, FAD can also be non-covalently bound as in the SQR of A. ferrooxidans and some other organisms.
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