User:Emma Ste.Marie/Sandbox 1: Difference between revisions

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Sec-mTrxR works by using a hydride from NADPH to reduce a bound flavin. The reduced flavin on one subunit reduces the conserved N-terminal disulfide redox center (CICVNVGCCT), which in turn reduces the 8-membered selenosulfide ring of the Cys1-Sec2 dyad that is attached to the enzyme through a flexible peptide linker on the opposite subunit[5-6]. Once the C-terminal selenosulfide is reduced, it passes its electrons to the disulfide bond of Trx, forming a senosulfide bond with Trx. This mTrxR-Trx selenosulfide bond is then resolved by attack of Cys1 on Sec2. This results in the formation of a rare 8-membered selenosulfide ring. This ring is subsequently attacked and re-opened by attack of Se in Sec2 from CysIC.  
Sec-mTrxR works by using a hydride from NADPH to reduce a bound flavin. The reduced flavin on one subunit reduces the conserved N-terminal disulfide redox center (CICVNVGCCT), which in turn reduces the 8-membered selenosulfide ring of the Cys1-Sec2 dyad that is attached to the enzyme through a flexible peptide linker on the opposite subunit[5-6]. Once the C-terminal selenosulfide is reduced, it passes its electrons to the disulfide bond of Trx, forming a senosulfide bond with Trx. This mTrxR-Trx selenosulfide bond is then resolved by attack of Cys1 on Sec2. This results in the formation of a rare 8-membered selenosulfide ring. This ring is subsequently attacked and re-opened by attack of Se in Sec2 from CysIC.  


[[Image:Twostepmechanism.png|700px|right|thumb|Mechanism of mTrxR1, described above.]]
[[Image:Twostepmechanism.png|500px|right|thumb|Mechanism of mTrxR1, described above.]]




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