Difference between revisions of "Part:BBa K3823001"
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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.
 
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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[[Image: BBa_K3823001-figure 1.png|thumb|center|800px|]]
  
  

Revision as of 09:39, 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.

BBa K3823001-figure 1.png


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]