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| {{enzyme
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| | Name = all-trans-retinol 13,14-reductase
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| | EC_number = 1.3.99.23
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| | CAS_number = 418767-56-3
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| | IUBMB_EC_number = 1/3/99/23
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| | GO_code = 0051786
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| {{Orphan|date=February 2009}}
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| In [[enzymology]], an '''all-trans-retinol 13,14-reductase''' ({{EC number|1.3.99.23}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
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| :all-trans-13,14-dihydroretinol + acceptor <math>\rightleftharpoons</math> all-trans-retinol + reduced acceptor
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| Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[all-trans-13,14-dihydroretinol]] and [[Electron acceptor|acceptor]], whereas its two [[product (chemistry)|products]] are [[all-trans-retinol]] and [[reduced acceptor]]. Under physiological conditions the reaction proceeds in the opposite direction catalyzing the saturation of the 13-14 double bond of [[all-trans-retinol]].
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| This enzyme belongs to the family of [[oxidoreductase]]s, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is '''all-trans-13,14-dihydroretinol:acceptor 13,14-oxidoreductase'''. Other names in common use include '''retinol saturase''', '''RetSat''', '''(13,14)-all-trans-retinol saturase''', and '''all-trans-retinol:all-trans-13,14-dihydroretinol saturase'''.
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| ==References==
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| {{reflist|1}}
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| * {{cite journal | author = Moise AR, Kuksa V, Imanishi Y, Palczewski K | year = 2004 | title = Identification of all-trans-retinol:all-trans-13,14-dihydroretinol saturase | journal = J. Biol. Chem. | volume = 279 | pages = 50230–42 | pmid = 15358783 | doi = 10.1074/jbc.M409130200 | issue = 48 | pmc = 2665716 }}
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| [[Category:EC 1.3.99]]
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| [[Category:Enzymes of unknown structure]]
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| {{1.3-enzyme-stub}}
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