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CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
retinol dehydrogenase <enzyme> 9-cis-retinol dehydrogenase is also available
Registry number: EC 1.1.1.105
Synonym: 11-cis retinol dehydrogenase, p32 retinol dehydrogenase
(26 Jun 1999)
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
9-cis-retinol dehydrogenase <enzyme> Catalyses oxidation of 9-cis-retinol to 9-cis-retinaldehyde; does not catalyze oxidation of all-trans-retinol; genbank u89717
Registry number: EC 1.1.1.-
Synonym: retinol dehydrogenase (9-cis)
(26 Jun 1999)
retinol Vitamin A1alcohol; 2,6,6-trimethyl-1-(9'-hydroxy-3',7'-dimethylnona-1',3',5',7'-tetraenyl)cyclohex-1-ene;a half-carotene bearing the b (or beta-ionone) form of the cyclic end group and a CH2OH at the C-15 position (numbering as in carotenoids) or 9'-position (numbering as a nonyl side chain on a cyclohexene ring); an intermediate in the vision cycle, it also plays a role in growth and differentiation.
See: dehydroretinol.
Synonym: vitamin A1 alcohol, vitamin A1.
Retinol dehydrogenase, an oxidoreductase catalyzing interconversion of retinal and NADH to retinol and NAD+.
(05 Mar 2000)
retinol 4-hydroxylase <enzyme> Converts retinol to 4-hydroxyretinol in presence of NADPH
Registry number: EC 1.14.13.-
(26 Jun 1999)
retinol-binding protein <molecular biology> Proteins which bind with retinol.
The retinol-binding protein found in plasma has an alpha-1 mobility on electrophoresis and a molecular weight of 21,000-22,000. The protein has one binding site for retinol and is responsible for the transport of vitamin A.
The retinol- protein complex (molecular weight 80,000 to 90,000) circulates in plasma in the form of a protein-protein complex with prealbumin. The retinol-binding protein found in tissue has a molecular weight of 14,000 and carries retinol as a non-covalently-bound ligand.
(03 Jul 1999)
retinol dehydratase <enzyme> Catalyses conversion of retinol to anhydroretinol; isolated from spodoptera frugiperda; genbank u28654
Registry number: EC 4.2.1.-
(26 Jun 1999)
retinol isomerase <enzyme> Catalyses the isomerization of all trans-retinol to 11-cis-retinol in the dark; found in the pigment epithelium in the eye
Registry number: EC 5.2.1.7
Synonym: retinoid isomerase
(26 Jun 1999)
11-cis-retinol Retinol with cis configuration at the 11-position (carotenoid numbering) or 5'-position (retinol numbering) of the side chain; an intermediate in the vision cycle.
Synonym: neoretinene B.
(05 Mar 2000)
lecithin-retinol acyltransferase <enzyme> Transfers 1-acyl moiety from lecithin to retinol-cellular retinol-binding protein, type II, to produce retinyl esters; does not use CoA
Registry number: EC 2.3.1.-
(26 Jun 1999)
acetaldehyde dehydrogenase <enzyme> Works with both nad and nadp
Registry number: EC 1.2.1.5
Synonym: aldehyde dehydrogenase (NADP+), naho gene product
(26 Jun 1999)
acetoin dehydrogenase <enzyme> An enzyme that catalyses the conversion of acetoin to diacetyl in the presence of NAD.
Chemical name: Acetoin:NAD+ oxidoreductase
Registry number: EC 1.1.1.5
(12 Dec 1998)
acetol dehydrogenase <enzyme> Forms methylglyoxal; uses nad+
Registry number: EC 1.1.1.-
Synonym: 1-hydroxyacetone dehydrogenase
(26 Jun 1999)
acyl-ACP dehydrogenase enoyl-ACP reductase (NADPH)
acyl-CoA dehydrogenase <enzyme> See also records for specific fatty acyl groups which have full EC nomenclature number; electron-transferring flavoprotein system reducing ubiquinone and other acceptors; formerly EC 1.3.2.2
Registry number: EC 1.3.99.3
Synonym: fatty-acyl CoA dehydrogenase, palmitoyl-CoA dehydrogenase, short-chain acyl-CoA dehydrogenase, acyl-coenzyme a dehydrogenase, lauroyl-CoA oxidase
(26 Jun 1999)
acyl-CoA dehydrogenase (NADPH+) Enzyme catalyzing the reversible reduction of enoyl-CoA derivatives of chain length 4 to 16, with NADPH as the hydrogen donor, forming acyl-CoA and NADP+.
Synonym: enoyl-CoA reductase.
(05 Mar 2000)
alanopine dehydrogenase <enzyme> Catalyses reductive elimination between pyruvate and alanine, or glycine, utilizing NADH as coenzyme, producing 2,2'-iminodipropionic acid (alanopine)
Registry number: EC 1.5.1.-
(26 Jun 1999)
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