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

BRENDA support

Literature summary extracted from

  • Jia, B.; Jia, X.; Hyun Kim, K.; Ji Pu, Z.; Kang, M.S.; Ok Jeon, C.
    Evolutionary, computational, and biochemical studies of the salicylaldehyde dehydrogenases in the naphthalene degradation pathway (2017), Sci. Rep., 7, 43489 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.65 sequence comparisons and phylogenetic tree, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli Alteromonas naphthalenivorans

Protein Variants

EC Number Protein Variants Comment Organism
1.2.1.65 E175A site-directed mutagenesis, the apparent Km value of the mutant enzyme to NAD+ is increased by about 2times and the kcat/Km toward the cofactor decreased by 4times. The Km value of the mutant toward salicylaldehyde also increases and the catalytic efficiency decreases by 6times compared to the wild-type enzyme Alteromonas naphthalenivorans
1.2.1.65 additional information site-directed mutagenesis of selected residues binding NAD+ and/or SAL affects the enzyme's catalytic efficiency, but does not eliminate catalysis Alteromonas naphthalenivorans
1.2.1.65 N149A site-directed mutagenesis, the catalyic efficiency of the mutant is decreased compared to the wild-type enzyme Alteromonas naphthalenivorans
1.2.1.65 V153A site-directed mutagenesis, the mutation has no significant effect on the kinetic parameters for either NAD+ or salicylaldehyde compared to the wild-type enzyme Alteromonas naphthalenivorans

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.65 Salicylaldehyde substrate inhibition Alteromonas naphthalenivorans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.65 additional information
-
 additional information bisubstrate Michaelis-Menten kinetics Alteromonas naphthalenivorans
1.2.1.65 0.0038
-
 Salicylaldehyde pH 7.5, 35°C, recombinant His-tagged enzyme Alteromonas naphthalenivorans
1.2.1.65 0.0046
-
 Salicylaldehyde pH 7.5, 35°C, recombinant His-tagged mutant V153A Alteromonas naphthalenivorans
1.2.1.65 0.0095
-
 Salicylaldehyde pH 7.5, 35°C, recombinant His-tagged mutant V153A Alteromonas naphthalenivorans
1.2.1.65 0.0151
-
 Salicylaldehyde pH 7.5, 35°C, recombinant His-tagged mutant E175A Alteromonas naphthalenivorans
1.2.1.65 0.0395
-
 NAD+ pH 7.5, 35°C, recombinant His-tagged enzyme Alteromonas naphthalenivorans
1.2.1.65 0.0449
-
 NAD+ pH 7.5, 35°C, recombinant His-tagged mutant N149A Alteromonas naphthalenivorans
1.2.1.65 0.0523
-
 NAD+ pH 7.5, 35°C, recombinant His-tagged mutant N149A Alteromonas naphthalenivorans
1.2.1.65 0.1056
-
 NAD+ pH 7.5, 35°C, recombinant His-tagged mutant E175A Alteromonas naphthalenivorans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.65 160000
-
 recombinant His-tagged enzyme, gel filtration Alteromonas naphthalenivorans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.65 salicylaldehyde + NAD+ + H2O Alteromonas naphthalenivorans
-
 salicylate + NADH + 2 H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.65 Alteromonas naphthalenivorans F5Z5S7
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.65 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography Alteromonas naphthalenivorans

Reaction

EC Number Reaction Comment Organism Reaction ID
1.2.1.65 salicylaldehyde + NAD+ + H2O = salicylate + NADH + 2 H+ catalytic mechanism, overview Alteromonas naphthalenivorans
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.65 salicylaldehyde + NAD+ + H2O
-
 Alteromonas naphthalenivorans salicylate + NADH + 2 H+
-
 ?
1.2.1.65 salicylaldehyde + NAD+ + H2O amino acids Asn149 and Glu250 may bind salicylaldehyde Alteromonas naphthalenivorans salicylate + NADH + 2 H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.1.65 homotrimer 3 * 53000, recombinant His-tagged enzyme, SDS-PAGE Alteromonas naphthalenivorans
1.2.1.65 More substrate binding induces a conformational change. SALDan three-dimensional homology modeling using the crystal structures of SALDpp, PDB ID 4JZ6, and other aldehyde dehydrogenases, PDB IDs 4FR8, 4O6R, 4NMK, 2O2P, and 3PQA, as model structures Alteromonas naphthalenivorans

Synonyms

EC Number Synonyms Comment Organism
1.2.1.65 SAL dehydrogenase
-
 Alteromonas naphthalenivorans
1.2.1.65 SALD
-
 Alteromonas naphthalenivorans
1.2.1.65 SALDan
-
 Alteromonas naphthalenivorans

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.2.1.65 25 35 high activity within this range Alteromonas naphthalenivorans

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2.1.65 82.2
-
 Salicylaldehyde pH 7.5, 35°C, recombinant His-tagged mutant E175A Alteromonas naphthalenivorans
1.2.1.65 100.4
-
 Salicylaldehyde pH 7.5, 35°C, recombinant His-tagged mutant N149A Alteromonas naphthalenivorans
1.2.1.65 123.6
-
 Salicylaldehyde pH 7.5, 35°C, recombinant His-tagged enzyme Alteromonas naphthalenivorans
1.2.1.65 153.5
-
 Salicylaldehyde pH 7.5, 35°C, recombinant His-tagged mutant V153A Alteromonas naphthalenivorans
1.2.1.65 157.6
-
 NAD+ pH 7.5, 35°C, recombinant His-tagged mutant E175A Alteromonas naphthalenivorans
1.2.1.65 208.8
-
 NAD+ pH 7.5, 35°C, recombinant His-tagged mutant N149A Alteromonas naphthalenivorans
1.2.1.65 234.3
-
 NAD+ pH 7.5, 35°C, recombinant His-tagged enzyme Alteromonas naphthalenivorans
1.2.1.65 254.5
-
 NAD+ pH 7.5, 35°C, recombinant His-tagged mutant N149A Alteromonas naphthalenivorans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.65 7.5
-
-
 Alteromonas naphthalenivorans

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.2.1.65 6 9 high activity within this range Alteromonas naphthalenivorans

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.65 NAD+ amino acid residues Trp148, Phe226, Gly228, and Phe381 may bind NAD+, predicted binding mode based on modelling and molecular dynamic simulation. The adenine dinucleotide part of NAD+ is stabilized by Gly208, Glu209, Val212, Phe226, Gly228, Val232, Ile236, Glu379, and Phe381. The dinucleotide also forms a hydrogen bond with Lys172, Glu175, and Asn213. The nicotinamide of NAD+ interacts with Trp148 and Asn149 via hydrogen bond formation. Pro147, Leu251, and Gly252 contribute the binding by hydrophobic interactions. A conformational change occurred in the NAD+ binding site, which may facilitate NADH release Alteromonas naphthalenivorans

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.2.1.65 0.3787
-
 Salicylaldehyde pH 7.5, 35°C, recombinant His-tagged enzyme Alteromonas naphthalenivorans
1.2.1.65 0.4283
-
 Salicylaldehyde pH 7.5, 35°C, recombinant His-tagged mutant V153A Alteromonas naphthalenivorans
1.2.1.65 0.4467
-
 Salicylaldehyde pH 7.5, 35°C, recombinant His-tagged mutant N149A Alteromonas naphthalenivorans
1.2.1.65 0.4616
-
 Salicylaldehyde pH 7.5, 35°C, recombinant His-tagged mutant E175A Alteromonas naphthalenivorans

Expression

EC Number Organism Comment Expression
1.2.1.65 Alteromonas naphthalenivorans SALD from Alteromonas naphthalenivorans (SALDan) is specifically upregulated in response to naphthalene up

General Information

EC Number General Information Comment Organism
1.2.1.65 evolution network and phylogenetic analyses indicated that salicylaldehyde dehydrogenases (SALDs) and the homologues are present in bacteria and fungi, phylogenetic tree, distribution, and evolution of SALD, overview. Key residues in SALDs are analyzed by evolutionary methods and a molecular simulation analysis. The catalytic residue is most highly conserved, followed by the residues binding NAD+ and then the residues binding salicylaldehyde, molecular simulation analysis Alteromonas naphthalenivorans
1.2.1.65 malfunction site-directed mutagenesis of selected residues binding NAD+ and/or SAL affects the enzyme's catalytic efficiency, but does not eliminate catalysis. Cys284 is positioned close to both NAD+ and SAL, implicating it as a potentially important residue Alteromonas naphthalenivorans
1.2.1.65 metabolism the salicylaldehyde dehydrogenases is involved in the naphthalene degradation pathway Alteromonas naphthalenivorans
1.2.1.65 additional information substrate binding induces a conformational change Alteromonas naphthalenivorans
1.2.1.65 physiological function salicylaldehyde dehydrogenase is responsible for the oxidation of salicylaldehyde to salicylate using NAD+ as a cofactor in the naphthalene degradation pathway Alteromonas naphthalenivorans

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.2.1.65 1492
-
 NAD+ pH 7.5, 35°C, recombinant His-tagged mutant E175A Alteromonas naphthalenivorans
1.2.1.65 3992
-
 NAD+ pH 7.5, 35°C, recombinant His-tagged mutant N149A Alteromonas naphthalenivorans
1.2.1.65 5444
-
 Salicylaldehyde pH 7.5, 35°C, recombinant His-tagged mutant E175A Alteromonas naphthalenivorans
1.2.1.65 5668
-
 NAD+ pH 7.5, 35°C, recombinant His-tagged mutant N149A Alteromonas naphthalenivorans
1.2.1.65 5932
-
 NAD+ pH 7.5, 35°C, recombinant His-tagged enzyme Alteromonas naphthalenivorans
1.2.1.65 10568
-
 Salicylaldehyde pH 7.5, 35°C, recombinant His-tagged mutant N149A Alteromonas naphthalenivorans
1.2.1.65 32526
-
 Salicylaldehyde pH 7.5, 35°C, recombinant His-tagged enzyme Alteromonas naphthalenivorans
1.2.1.65 33370
-
 Salicylaldehyde pH 7.5, 35°C, recombinant His-tagged mutant V153A Alteromonas naphthalenivorans