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• W2052238907 abstract "DAhydratases have been DAtected in anaerobic bacteria which use 2‐, 4‐ or 5‐hydroxyacyl‐CoA as substrates and are involved in the removal of hydrogen atoms from the unactivated β‐ or γ‐positions. In addition there are bacterial DAhydratases acting on 1,2‐diols which are substrates lacking any activating group. These enzymes contain either FAD, or flavins + iron‐sulfur clusters or coenzyme B 12 . It has been proposed that the overall DAhydrations are actually reductions followed by oxidations or vice versa mediated by these prosthetic groups. Whereas the γ‐hydrogen of 5‐hydroxyvaleryl‐CoA is activated by a transient two‐electron α,β‐oxidation, the other substrates are proposed to require either a transient one‐electron reduction or an oxidation to a ketyl (radical anion)." @default.
• W2052238907 created "2016-06-24" @default.
• W2052238907 creator A5024196097 @default.
• W2052238907 date "1996-06-24" @default.
• W2052238907 modified "2023-10-16" @default.
• W2052238907 title "Unusual DAhydrations in anaerobic bacteria: considering ketyls (radical anions) as reactive intermediates in enzymatic reactions" @default.
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• W2052238907 doi "https://doi.org/10.1016/0014-5793(96)00530-3" @default.
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