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Literature summary extracted from

  • Liu, L.K.; Tanner, J.J.
    Crystal structure of aldehyde dehydrogenase 16 reveals trans-hierarchical structural similarity and a new dimer (2019), J. Mol. Biol., 431, 524-541 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.3 gene ALDH16, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Codon Plus Loktanella sp.

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.2.1.3 purified recombinant wild-type enzyme LsALDH16 and enzyme mutant C295A free or in complex with NAD+ or NADH or 4-nitrophenylacetate, hanging drop vapor diffusion, mixing of 6 mg/ml in 20 mM Tris-HCl, pH 8.0, 100 mM NaCl, 2.5% glycerol, and 0.5 mM tris(2-carboxyethyl)phosphine, with reservoir solution and microseeding solution in a volume ratio of 1:1:0.2, where the reservoir solution comprisess 20% w/v PEG 3350, 200 mM ammonium sulfate, and 100 mM Bis-Tris, pH 5.5, and the microseed solution is made from crushed crystals diluted 1:100 in reservoir, at room temperature, crystals of mutant C295A complexed with 4-nitrophenylacetate are prepared by soaking the apo crystals with the reservoir solution supplemented with 10 mM ligand for about 30 minutes, X-ray diffraction structure determination and analysis at 1.49-2.30 A resolution Loktanella sp.

Protein Variants

EC Number Protein Variants Comment Organism
1.2.1.3 C295A site-directed mutagenesis, inactive mutant Loktanella sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.3 4-nitrophenylacetate substrate inhibition of esterase activity Loktanella sp.
1.2.1.3 N,N-diethylaminobenzaldehyde DEAB, complete inhibition Loktanella sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.3 additional information
-
 additional information Michaelis-Menten kinetics and modeling Loktanella sp.
1.2.1.3 0.0213
-
 hexanal pH 8.0, 22°C, recombinant wild-type enzyme Loktanella sp.

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.3 Homo sapiens Q8IZ83
-
-
1.2.1.3 Loktanella sp.
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.3 recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) Codon Plus by nickel affinity chromatography, anion exchange chromatography, and gel filtration Loktanella sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.3 hexanal + NAD+ + H2O
-
 Loktanella sp. hexanoate + NADH + H+
-
 ?
1.2.1.3 additional information enzyme LsALDH16 also exhibits esterase activity with 4-nitrophenylacetate (pNPA) as substrate in the absence of NAD+, kinetics, overview Loktanella sp. ?
-
-
1.2.1.3 additional information no activity with hexanal, propanal, nonanal, acetaldehyde and aminoadipate semialdehyde Homo sapiens ?
-
-

Subunits

EC Number Subunits Comment Organism
1.2.1.3 dimer 2 * 80792, mass spectrometry Loktanella sp.
1.2.1.3 dimer 2 * 85395, mass spectrometry Homo sapiens
1.2.1.3 More the fold of ALDH16 comprises three domains: NAD+-binding, catalytic, and C-terminal. The latter is unique to ALDH16 and features a Rossmann fold connected to a protruding beta-flap. The tertiary structural interactions of the C-terminal domain mimic the quaternary structural interactions of the classic ALDH superfamily dimer, a phenomenon that is called trans-hierarchical structural similarity. ALDH16 forms a unique dimer in solution, which mimics the classic ALDH superfamily dimer-of-dimers tetramer Loktanella sp.
1.2.1.3 More the fold of ALDH16 comprises three domains: NAD+-binding, catalytic, and C-terminal. The latter is unique to ALDH16 and features a Rossmann fold connected to a protruding beta-flap. The tertiary structural interactions of the C-terminal domain mimic the quaternary structural interactions of the classic ALDH superfamily dimer, a phenomenon that is called trans-hierarchical structural similarity. ALDH16 forms a unique dimer in solution, which mimics the classic ALDH superfamily dimer-of-dimers tetramer Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.2.1.3 aldehyde dehydrogenase 16
-
 Loktanella sp.
1.2.1.3 aldehyde dehydrogenase 16
-
 Homo sapiens
1.2.1.3 ALDH16
-
 Loktanella sp.
1.2.1.3 ALDH16
-
 Homo sapiens
1.2.1.3 HsALDH16A1
-
 Homo sapiens
1.2.1.3 LsALDH16
-
 Loktanella sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.1.3 22
-
 assay at room temperature Loktanella sp.

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.1.3 3.3
-
 hexanal pH 8.0, 22°C, recombinant wild-type enzyme Loktanella sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.3 8
-
 assay at Loktanella sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.3 NAD+
-
 Homo sapiens
1.2.1.3 NAD+ enzyme binding analysis, overview Loktanella sp.

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.2.1.3 1.2
-
 4-nitrophenylacetate pH and temperature not specified in the publication Loktanella sp.

General Information

EC Number General Information Comment Organism
1.2.1.3 evolution the enzyme belongs to the aldehyde dehydrogenase (ALDH) superfamily. Enzyme ALDH16 has an extra C-terminal domain of unknown function and shows absence of the essential catalytic cysteine residue in certain non-bacterial ALDH16 sequences Homo sapiens
1.2.1.3 evolution the enzyme belongs to the aldehyde dehydrogenase (ALDH) superfamily. Enzyme ALDH16 has an extra C-terminal domain of unknown function and shows absence of the essential catalytic cysteine residue in certain non-bacterial ALDH16 sequences. The Loktanella ALDH16 structure may be considered to be the archetype of the ALDH16 family Loktanella sp.
1.2.1.3 additional information active site structure modeling of LsALDH16 from 1.65 A resolution crystal structure with the catalytic loop in complex with NAD+. Structure comparison of the human and the Loktanella sp. ALDH16 enzymes, overview Loktanella sp.
1.2.1.3 additional information structure comparison of the human and the Loktanella sp. ALDH16 enzymes, overview Homo sapiens
1.2.1.3 physiological function human ALDH16A1 apparently lacks measurable aldehyde oxidation activity, suggesting it is a pseudoenzyme, consistent with the absence of the catalytic Cys in its sequence Homo sapiens
1.2.1.3 physiological function Loktanella ALDH16 is a bona fide enzyme, exhibiting NAD+-binding Loktanella sp.

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.2.1.3 154.93
-
 hexanal pH 8.0, 22°C, recombinant wild-type enzyme Loktanella sp.