Image:Proposed enzymatic mechanism for the CBS.png
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Jan Hamalcik (Talk | contribs)
(Proposed enzymatic mechanism for the CBS reaction with absorption maxima. Possible quinonoid intermediates between E-serine (E-PLP-L-ser) and E-aminoacrylate (E-PLPaa) or between E-aminoacrylate and E-cystathionine are not shown. The growing consensus amo)
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Revision as of 19:46, 28 April 2019
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Proposed enzymatic mechanism for the CBS reaction with absorption maxima. Possible quinonoid intermediates between E-serine (E-PLP-L-ser) and E-aminoacrylate (E-PLPaa) or between E-aminoacrylate and E-cystathionine are not shown. The growing consensus among those working on fold type-II PLP-dependent enzymes is that the ring nitrogen does not undergo protonation during the catalytic cycle in these enzymes. However, at pH 6.5 the expectation is that the ring nitrogen is protonated as shown.
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| Date/Time | User | Dimensions | File size | Comment | |
|---|---|---|---|---|---|
| (current) | 19:46, 28 April 2019 | Jan Hamalcik (Talk | contribs) | 990×590 | 122 KB | Proposed enzymatic mechanism for the CBS reaction with absorption maxima. Possible quinonoid intermediates between E-serine (E-PLP-L-ser) and E-aminoacrylate (E-PLPaa) or between E-aminoacrylate and E-cystathionine are not shown. The growing consensus amo |
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