File:Proposed enzymatic mechanism for the CBS.png
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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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PMID: 29630349
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| Date/Time | Thumbnail | Dimensions | User | Comment | |
|---|---|---|---|---|---|
| current | 19:46, 28 April 2019 | | 990 × 590 (122 KB) | 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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