Literature summary for 1.2.1.65 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 .

Search for more literature for 1.2.1.65

Cloned(Commentary)

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

Protein Variants

Protein Variants	Comment	Organism
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
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
N149A	site-directed mutagenesis, the catalyic efficiency of the mutant is decreased compared to the wild-type enzyme	Alteromonas naphthalenivorans
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

Inhibitors	Comment	Organism	Structure
Salicylaldehyde	substrate inhibition	Alteromonas naphthalenivorans

KM Value [mM]

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Alteromonas naphthalenivorans	F5Z5S7	-	-

Purification (Commentary)

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

Reaction

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

Substrates and Products (Substrate)

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

Subunits

Subunits	Comment	Organism
homotrimer	3 * 53000, recombinant His-tagged enzyme, SDS-PAGE	Alteromonas naphthalenivorans
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

Synonyms	Comment	Organism
SAL dehydrogenase	-	Alteromonas naphthalenivorans
SALD	-	Alteromonas naphthalenivorans
SALDan	-	Alteromonas naphthalenivorans

Temperature Range [°C]

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

Turnover Number [1/s]

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

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	-	Alteromonas naphthalenivorans

pH Range

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

Cofactor

Cofactor	Comment	Organism	Structure
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]

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

Expression

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

General Information

General Information	Comment	Organism
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
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
metabolism	the salicylaldehyde dehydrogenases is involved in the naphthalene degradation pathway	Alteromonas naphthalenivorans
additional information	substrate binding induces a conformational change	Alteromonas naphthalenivorans
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]

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

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Release 2023.1 (January 2023)