Literature summary for 1.2.1.5 extracted from

Jung, K.; Hong, S.H.; Ngo, H.P.; Ho, T.H.; Ahn, Y.J.; Oh, D.K.; Kang, L.W.
Crystal structures of an atypical aldehyde dehydrogenase having bidirectional oxidizing and reducing activities (2017), Int. J. Biol. Macromol., 105, 816-824 .

Application

Application	Comment	Organism
synthesis	the enzyme can be useful in the production of retinoic acid and related high-end products	Bacillus cereus

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant tagged enzyme expression in Escherichia coli strain ER2566	Bacillus cereus

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Bacillus cereus

Crystallization (Comment)

Organism

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

Bacillus cereus

Organism

Organism	UniProt	Comment	Textmining
Bacillus cereus	A0A150BLG9	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant tagged enzyme from Escherichia coli strain ER2566 by metal chelating affinity chromatography, desalting gel filtration, and dialysis	Bacillus cereus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
acetaldehyde + NAD(P)+ + H2O	-	Bacillus cereus	acetate + NAD(P)H + H+	-	?
all-trans-retinal + NAD+	-	Bacillus cereus	all-trans-retinol + NADH + H+	-	?
all-trans-retinal + NADP+	-	Bacillus cereus	all-trans-retinol + NADPH + H+	-	?
all-trans-retinol + NAD+ + H2O	-	Bacillus cereus	all-trans-retinoic acid + NADH + H+	-	?
all-trans-retinol + NADP+ + H2O	-	Bacillus cereus	all-trans-retinoic acid + NADPH + H+	-	?
benzaldehyde + NAD(P)+ + H2O	-	Bacillus cereus	benzoate + NAD(P)H + H+	-	?
additional information	in the first acylation step, the activated catalytic Cys, Cys300 in BcALDH, attacks the substrate aldehyde group to form a thio-hemiacetal intermediate. The oxidized NAD(P)+ cofactor takes up a hydride ion from the thio-hemiacetal intermediate, which transforms it to a thioester intermediate. This intermediate is then deacylated by a water molecule, in which the additional catalytic residue Glu, Glu266 in BcALDH, activates the hydrolytic water molecule by abstracting a proton. Finally, the reduced NAD(P)H is released. Plausible mechanism for the minor reducing activity of BcALDH with all-trans-retinal, overview. The beta-ionone ring of the superimposed retinoic acid (REA) is bound at the mouth of the channel and exposed to the solvent. The substrate binding pocket-bound REA shows a bent conformation in the carbon positions from 9 to 11. Molecular docking of retinoic acid into the enzyme structure. BcALDH has a strict substrate preference for oxidation of all-trans-retinal, with no activity detected against 9-cis-retinal and 13-cis-retinal. BcALDH also has 14 and 30fold lower Km values for all-trans-retinal compared to the small aldehydes acetaldehyde and benzaldehyde, respectively	Bacillus cereus	?	-	-

Synonyms

Synonyms	Comment	Organism
BcALDH	-	Bacillus cereus
More	see also EC 1.2.1.36	Bacillus cereus

Cofactor

Cofactor	Comment	Organism
additional information	the nicotinamide moieties of NAD+ and NADP+ directly interact with the conserved catalytic residues Cys300 and Glu266, and binding causes concerted conformational changes. Flexible cofactor-binding pocket of BcALDH. Cofactor-enzyme binding structure analysis, overview	Bacillus cereus
NAD+	-	Bacillus cereus
NADP+	-	Bacillus cereus

General Information

General Information	Comment	Organism
additional information	enzyme structure comparisons, overview	Bacillus cereus
physiological function	enzyme BcALDH is an atypical aldehyde dehydrogenase having bidirectional oxidizing and reducing activities	Bacillus cereus