Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

1.2.1.36: retinal dehydrogenase

This is an abbreviated version!
For detailed information about retinal dehydrogenase, go to the full flat file.

Word Map on EC 1.2.1.36

Reaction

retinal
+
NAD+
 +
H2O
=
retinoate
 +
NADH
 +
H+

Synonyms

aldehyde dehydrogenase 1, aldehyde dehydrogenase 1A1, aldehyde dehydrogenase 1A2, aldehyde dehydrogenase 1A3, ALDH 1A1, ALDH 1A2, ALDH class 1, ALDH-1A1, ALDH-3A1, ALDH1, ALDH1A1, Aldh1a2, Aldh1a3, BcALDH, cytosolic retinal dehydrogenase, dehydrogenase, retinal, dehydrogenase/reductase member 3, DHRS3, ETA-crystallin, More, NAD+-dependent aldehyde dehydrogenase, NAD-dependent retinal dehydrogenase, NAD-dependent retinal dehydrogenases, PB-RALDH, phenobarbital-induced aldehyde dehydrogenase, RALDH, RALDH-1, RALDH-3, RalDH1, RALDH1A1, RALDH2, RALDH3, Raldh4, RDH12, RDH13, RDH5, retialdehyde dehydrogenase, Retinal dehydrogenase, retinal dehydrogenase 1, retinal dehydrogenase 2, retinal dehydrogenase 3, retinal dehydrogenase 4, retinal dehydrogenase 5, retinal dehydrogenase type-2, retinal dehydrogenase-2, retinal dehydrogenase/reductase, retinal short-chain dehydrogenase/reductase, retinalaldehyde dehydrogenase 2, retinaldehyde dehydrogenase, retinaldehyde dehydrogenase 1, retinaldehyde dehydrogenase 2, retinaldehyde dehydrogenase 3, retinaldehyde dehydrogenase type II, retinaldehyde dehydrogenase type-1, retinaldehyde dehydrogenase-2, retinaldehyde dehydrogenases, retinol dehydrogenase 13, retSDR1, testis-specific aldehyde dehydrogenase, thyroid-hormone-binding protein, type 2 retinaldehyde dehydrogenase, xCTBP, xCTBP/xALDH1, zRalDH

ECTree

     1 Oxidoreductases
         1.2 Acting on the aldehyde or oxo group of donors
             1.2.1 With NAD+ or NADP+ as acceptor
                1.2.1.36 retinal dehydrogenase

Crystallization

Crystallization on EC 1.2.1.36 - retinal dehydrogenase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant BcALDH alone and in complex with NAD+ and NADP+ cofactors, sitting drop vapour diffusion method, mixing of 10 mg/ml protein in 25 mM Tris, pH 7.5, 15 mM NaCl, and 3 mM 2-mercaptoethanol, with crystallization solution containing 0.15 M DL-malic acid, pH 7.0, and 18% PEG 3350 w/v, at 14°C, 1 week, X-ray diffraction structure determination and analysis at 2.0-2.6 A resolution, molecular replacement using human ALDH2 structure (PDB ID 4FR8) as the search model, modeling. The apo-BcALDH structure contains four protomers in the asymmetric unit
hanging drop vapor diffusion
purified enzyme in complex with inhibitors 2,3,5-trimethyl-6-[3-oxo-3-(piperidin-1-yl)propyl]-7H-furo[3,2-g][1]benzopyran-7-one, 7-(diethylamino)-4-methyl-2H-1-benzopyran-2-one, and 3-benzyl-4-methyl-2-oxo-2H-1-benzopyran-7-yl methanesulfonate, X-ray diffraction structure determination and analysis at 1.70-2.05 A resolution
recombinant isozyme type-2 mutant L459F/N460G in complex with NAD+ and in absence of substrate, hanging drop vapour diffusion method, 7.6 mg/ml enzyme with 2 mM NAD+ and about 14 mg/ml retinol, 0.002 ml protein solution plus equal volume of well solution containing 7% PEG 6000, 2% 2-methyl-2,4-pentanediol, and 0.1 M Tris, pH 7.5, X-ray diffraction structure determination and analysis at 3.3 A resolution
-