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

BRENDA support

1.2.1.5: aldehyde dehydrogenase [NAD(P)+]

This is an abbreviated version!
For detailed information about aldehyde dehydrogenase [NAD(P)+], go to the full flat file.

Word Map on EC 1.2.1.5

Reaction

an aldehyde
+
NAD(P)+
+
H2O
=
a carboxylate
+
NAD(P)H
+
H+

Synonyms

acetaldehyde dehydrogenase, ALD4, aldehyde dehydrogenase, aldehyde dehydrogenase 1A3, aldehyde dehydrogenase 2, aldehyde dehydrogenase 3A1, aldehyde: NAD(P)+ oxidoreductase, ALDH, ALDH1, ALDH13, ALDH17, ALDH1a, ALDH1A1, Aldh1a3, ALDH1b, ALDH2, ALDH2a, ALDH2b, ALDH3, ALDH3A1, Aldh3b1, ALDH3F1, ALDH3H1, ALDH3I1, ALDH7B7, ALDH9, ALDHC, ALDHIII, BcALDH, BCP54, chromosomally encoded box pathway ALDH, class 3 aldehyde dehydrogenase, Corneal 15.8 kDa protein, Corneal protein 54, dehydrogenase, aldehyde (nicotinamide adenine dinucleotide (phosphate)), HTC-ALDH, K-ACDH, MI dehydrogenase, More, myo-inositol dehydrogenase, NAD(P)(+)-dependent aldehyde dehydrogenase, NAD(P)+-dependent aldehyde dehydrogenase, NAD+-dependent Ald4, nicotinprotein aldehyde dehydrogenase, OsALDH2-1, OsALDH2-2, OsALDH2-3, OsALDH2-4, OsALDH2-5, OsALDH22, OsALDH3-1, OsALDH3-2, OsALDH3-3, OsALDH3-4, OsALDH3-5, OsALDH5, OsALDH7, PEG-ALDH, PuuC, ST0064, succinic semialdehyde dehydrogenase, Transparentin, Tumor-associated aldehyde dehydrogenase, ybcD

ECTree

     1 Oxidoreductases
         1.2 Acting on the aldehyde or oxo group of donors
             1.2.1 With NAD+ or NADP+ as acceptor
                1.2.1.5 aldehyde dehydrogenase [NAD(P)+]

Crystallization

Crystallization on EC 1.2.1.5 - aldehyde dehydrogenase [NAD(P)+]

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.15 M DL-malic acid pH 7.0, 18% (w/v) PEG 3350
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
the apoenzyme is crystallized by using 100 mM ACES, pH 6.4, 100-200 mM guanidine-HCl, 1-10 mM MgCl2 and 16–17% (w/v) PEG 6000, the mutant T244A in complex with NAD is crystallized by using 100 mM ACES, pH 6.4, 100 mM guanidine–HCl, 10 mM MgCl2 and 18% (w/v) PEG 6000
-
ALDHC in complex with NADPH bound in the cofactor binding pocket and an ordered fragment of a polyethylene glycol molecule bound in the substrate tunnel, to 1.6 A resolution. Belongs to space group P1. The ALDHC monomer comprises three distinct domains, an N-terminal cofactor (NAD/P+)-binding domain, a catalytic domain, and an oligomerization domain