1.1.1.2: alcohol dehydrogenase (NADP+)

This is an abbreviated version, for detailed information about alcohol dehydrogenase (NADP+), go to the full flat file.

Reaction

a primary alcohol
+
NADP+
=
an aldehyde
+
NADPH
+
H+

Synonyms

2° Adh, 3-DG-reducing enzyme, AAur_2040, ADH, ADH-1, ADH-2, ADH-I, ADH-II, ADH2, Adh319, ADH4, Adh6, AdhA, AdhB, AKR1A1, AKR1A4, alcohol dehydrogenase C, alcohol dehydrogenase [NADP(+)], Alcohol dehydrogenase [NADP+], aldehyde reductase, aldehyde reductase (NADPH2), aldehyde/ketone reductase, aldo-keto reductase, Aldo-keto reductase family 1 member A1, aldose reductase, ALDR, alipathic aldehyde reductase, ALR, ALR 1, ALR1, BdhA, bovine brain aldehyde reductase, D-glucuronate reductase, daunorubicin reductase, DRD, EhADH1, Gre2p, hexogenate dehydrogenase, high-Km aldehyde reductase, HvADH2, L-hexonate dehydrogenase, LB-RADH, LBADH, liver alcohol dehydrogenase, low-Km aldehyde reductase, mevaldate reductase, Mpd1, NADP(H)-dependent alcohol dehydrogenase, NADP-alcohol dehydrogenase, NADP-aldehyde reductase, NADP-dependent aldehyde reductase, NADP-linked aryl alcohol dehydrogenase, NADPH-aldehyde reductase, NADPH-cytochrome c reductase, NADPH-dependent aldehyde reductase, NADPH-dependent FALDR, NADPH-dependent fatty aldehyde reductase, NADPH-linked aldehyde reductase, nonspecific succinic semialdehyde reductase, Octopine dehydrogenase, putative iron alcohol dehydrogenase, PyAeADHII, rabbit kidney aldehyde-ketone reductase, RADH, ScADHVI, short-chain ADH, short-chain alcohol dehydrogenase, short-chain dehydrogenase/reductase, TBADH, TbADH1, Teth39_1597, Teth514_0564, TPN-L-hexonate dehydrogenase, TPNH-linked aldehyde reductase, TPNH-specific aldehyde reductase, triphosphopyridine nucleotide-linked aldehyde reductase, TsAdh319, Y63 protein, yeast alcohol dehydrogenase, YqhD

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.2 alcohol dehydrogenase (NADP+)

Crystallization

Crystallization on EC 1.1.1.2 - alcohol dehydrogenase (NADP+)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals of D275P–EhADH1 are grown using the hanging-drop vapor-diffusion method at 20°C. Crystal structure of the thermostabilized mutant D275P-EhADH1 suggests that a proline residue at position 275 thermostabilizes the enzymes by reducing flexibility and by reinforcing hydrophobic interactions at the dimer–dimer interface of the tetrameric ADH
16°C, wild-type RADH: 15 mg/ml stock solution (21% polyethyleneglycol monomethyl ether 550, 0.1 M Tris-HCl, 50 nM MgCl2, 40 mM acetophenone, 10 mM NADP+), growth for 3 weeks, max. size 0.25 mm x 0.25 mm x 1.0 mm, RADH-G37D: 21 mg/ml stock solution (methyl-2,4-pentanediol, 20% polyethyleneglycol 400 or polyethyleneglycol monomethyl ether 550, 0.1 M Hepes, 50 mM MgCl2 59 mM 1-phenylethanol, 25 mM NADH), growth 1 week, max. size 0.4 mm x 0.5 mm x 1.7 mm
-
modelling of NADPH and acetophenone into the active site
-
both in presence and absence of NADP+
-
in presence and absence of NADP+, structural features of an independent ADH class
-
sitting drop vapour diffusion plates at 20°C. Crystal structure and X-ray fluorescence of wild-type and cobalt-substituted enzyme. Cocrystal structure of the enzyme with NADPH and analysis of the putative active site
-
in complex with NADP+, to 3.2 A resolution. Crystals belong to space group P21
-
at 22°C by vapor-diffusion using the hanging drop method. ALR1 in ternary complex with the coenzyme NADPH and 3,5-dichlorosalicylic acid, at a resolution of 2.41 A
-
hanging drop method, with NADPH, ammonium sulfate, Tris HCl-buffer, pH 8.1, buffer C, maximum side: 0.3 mm x 0.1 mm x 0,1 mm after 1 week
-
in ternary complex with NADPH and a 5-arylidene-2,4-thiazolidinedione aldose reductase inhibitor, [5-(3-carboxymethoxy-4-methoxybenzylidene)-2,4-dioxothiazolidin-3-yl]acetic acid to 1.99 A resolution. The partially disordered inhibitor forms a tight network of hydrogen bonds with the active site residues Tyr50 and His113 and coenzyme. pi-Stacking interactions with several conserved active site tryptophan residues and hydrogen-bonding interactions with the non-conserved C-terminal residue Pro301 in aldehyde reductase ALR1 contribute to inhibitor selectivity. In particular for the potent inhibitor [5-(3-carboxymethoxy-4-methoxybenzylidene)-2,4-dioxothiazolidin-3-yl]acetic acid, the rotameric state of the conserved residue Trp220 in ALR1, i.e Trp 219 in aldose reductase, is important in forming a pi-stacking interaction with the inhibitor in aldose reductase and contributes to the difference in the binding of the inhibitor to the enzymes; purified aldehyde reductase, ALR1, in ternary complex with NADPH and [5-(3-carboxymethoxy-4-methoxybenzylidene)-2,4-dioxothiazolidin-3-yl]acetic acid, hanging drop method, 17-18 mg/ml protein in 5 mM Tris-HCl, pH 6.5, containing 5 mM 2-mercaptoethanol, mixed with NADPH and inhibitor in a 1:20:3molar ratio, the reservoir solution contains 2.0 M ammonium sulfate, and 0.1 M Tris-HCl buffer, pH 8.5, 10 days, X-ray diffraction structure determination and analysis at 1.99 A resolution
-
crystals of P275D–TbADH1 are grown using the hanging-drop vapor-diffusion method at 20°C. Crystal structure of the thermostabilized mutant P275D-EhADH1 suggests that a proline residue at position 275 thermostabilizes the enzymes by reducing flexibility and by reinforcing hydrophobic interactions at the dimer–dimer interface of the tetrameric ADH
crystal structure of the enzyme in a binary complex with 5-hydroxy-NADP at 1.68 A resolution
-
to 1.68 A resolution, crystals belong to space group I222, with unit-cell parameters a = 55.63, b = 83.25, c = 120.75 A
-