Literature summary for 1.2.1.19 extracted from

Kopecny, D.; Koncitikova, R.; Tylichova, M.; Vigouroux, A.; Moskalikova, H.; Soural, M.; Sebela, M.; Morera, S.
Plant ALDH10 family identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate (2013), J. Biol. Chem., 288, 9491-9507 .

Cloned(Commentary)

Cloned (Comment)	Organism
isozyme SlAMADH1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis	Solanum lycopersicum
isozyme SlAMADH2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis	Solanum lycopersicum
isozyme ZmAMADH1a, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis	Zea mays
isozyme ZmAMADH1b, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis	Zea mays
isozyme ZmAMADH2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis	Zea mays

Crystallization (Commentary)

Crystallization (Comment)	Organism
wild-type SlAMADH1 with 5 mM NAD+is crystallized over a reservoir containing 23% PEG 1000, 0.1 M HEPES, pH 7.5, mutant E260A of SlAMADH1 with 5 mM NAD+ is crystallized over a reservoir containing 15% PEG 1500, 0.1 M imidazole, pH 7.0, and 10% glycerol, sitting drop vapor diffusion method, cryoprotectant solution consits of mother liquor supplemented with 25% PEG 400 for SlAMADH1 or 20% glycerol for the E260A mutant, X-ray diffraction structure determination and analysis at 1.90 A resolution, molecular replacement method using the dimer structure of PsAMADH2, PDB ID 3IWJ, as a search model	Solanum lycopersicum
wild-type ZnAMADH1a with 5 mM NAD+ is crystallized over a reservoir containing 16% PEG 4000, 0.1 M HEPES, pH 7.5, and 10% isopropyl alcohol, sitting drop vapor diffusion method, cryoprotection by 20% glycerol in mother liquor, X-ray diffraction structure determination and analysis at 1.95 A resolution, molecular replacement method using the dimer structure of PsAMADH2, PDB ID 3IWJ, as a search model	Zea mays

Crystallization (Comment)

Organism

wild-type SlAMADH1 with 5 mM NAD+is crystallized over a reservoir containing 23% PEG 1000, 0.1 M HEPES, pH 7.5, mutant E260A of SlAMADH1 with 5 mM NAD+ is crystallized over a reservoir containing 15% PEG 1500, 0.1 M imidazole, pH 7.0, and 10% glycerol, sitting drop vapor diffusion method, cryoprotectant solution consits of mother liquor supplemented with 25% PEG 400 for SlAMADH1 or 20% glycerol for the E260A mutant, X-ray diffraction structure determination and analysis at 1.90 A resolution, molecular replacement method using the dimer structure of PsAMADH2, PDB ID 3IWJ, as a search model

Solanum lycopersicum

wild-type ZnAMADH1a with 5 mM NAD+ is crystallized over a reservoir containing 16% PEG 4000, 0.1 M HEPES, pH 7.5, and 10% isopropyl alcohol, sitting drop vapor diffusion method, cryoprotection by 20% glycerol in mother liquor, X-ray diffraction structure determination and analysis at 1.95 A resolution, molecular replacement method using the dimer structure of PsAMADH2, PDB ID 3IWJ, as a search model

Zea mays

Inhibitors

Inhibitors	Comment	Organism
3-aminopropanal	substrate inhibition; substrate inhibition	Solanum lycopersicum
4-aminobutanal	substrate inhibition	Solanum lycopersicum
4-guanidinobutyraldehyde	substrate inhibition; substrate inhibition	Solanum lycopersicum
additional information	no substrate inhibition by betaine aldehyde, 3-pyridine carboxaldehyde, 4-pyridine carboxaldehyde, and 4-aminobutanal	Solanum lycopersicum
N,N,N-trimethyl-4-aminobutyraldehyde	substrate inhibition; substrate inhibition	Solanum lycopersicum

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
0.003	-	4-guanidinobutyraldehyde	pH 9.0, 37°C	Zea mays
0.005	-	4-guanidinobutyraldehyde	pH 9.0, 37°C	Zea mays
0.006	-	N,N,N-trimethyl-4-aminobutyraldehyde	pH 9.0, 37°C	Zea mays
0.009	-	3-aminopropanal	pH 9.0, 37°C	Zea mays
0.009	-	3-aminopropanal	pH 9.0, 37°C	Solanum lycopersicum
0.01	-	N,N,N-trimethyl-4-aminobutyraldehyde	pH 9.0, 37°C	Zea mays
0.011	-	4-guanidinobutyraldehyde	pH 9.0, 37°C	Zea mays
0.011	-	3-aminopropanal	pH 9.0, 37°C	Zea mays
0.014	-	Betaine aldehyde	pH 9.0, 37°C	Zea mays
0.016	-	N,N,N-trimethyl-4-aminobutyraldehyde	pH 9.0, 37°C	Zea mays
0.017	-	N,N,N-trimethyl-4-aminobutyraldehyde	pH 9.0, 37°C	Solanum lycopersicum
0.022	-	4-guanidinobutyraldehyde	pH 9.0, 37°C	Solanum lycopersicum
0.026	-	4-aminobutanal	pH 9.0, 37°C	Zea mays
0.028	-	4-aminobutanal	pH 9.0, 37°C	Zea mays
0.029	-	Betaine aldehyde	pH 9.0, 37°C	Zea mays
0.041	-	3-aminopropanal	pH 9.0, 37°C	Solanum lycopersicum
0.05	-	4-pyridine carboxaldehyde	pH 9.0, 37°C	Solanum lycopersicum
0.054	-	4-aminobutanal	pH 9.0, 37°C	Solanum lycopersicum
0.059	-	4-aminobutanal	pH 9.0, 37°C	Zea mays
0.072	-	NAD+	pH 9.0, 37°C	Solanum lycopersicum
0.079	-	NAD+	pH 9.0, 37°C	Zea mays
0.085	-	4-guanidinobutyraldehyde	pH 9.0, 37°C	Solanum lycopersicum
0.086	-	NAD+	pH 9.0, 37°C	Zea mays
0.089	-	NAD+	pH 9.0, 37°C	Solanum lycopersicum
0.091	-	NAD+	pH 9.0, 37°C	Zea mays
0.098	-	3-aminopropanal	pH 9.0, 37°C	Zea mays
0.141	-	N,N,N-trimethyl-4-aminobutyraldehyde	pH 9.0, 37°C	Solanum lycopersicum
0.278	-	4-aminobutanal	pH 9.0, 37°C	Solanum lycopersicum
0.316	-	3-pyridine carboxaldehyde	pH 9.0, 37°C	Solanum lycopersicum
2.051	-	Betaine aldehyde	pH 9.0, 37°C	Solanum lycopersicum

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cytosol	probably, SlAMADH1 ends with a tripeptide SKN, which is not a peroxisomal targeting signal	Solanum lycopersicum	5829	-
peroxisome	the isozyme carries the SKL C-terminal peroxisomal targeting signal (PTS-1)	Zea mays	5777	-
peroxisome	the isozyme carries the SKL C-terminal peroxisomal targeting signal (PTS-1)	Solanum lycopersicum	5777	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
3-aminopropanal + NAD+ + H2O	Solanum lycopersicum	-	3-aminopropanoate + NADH + H+	-	?
3-aminopropanal + NAD+ + H2O	Zea mays	-	3-aminopropanoate + NADH + H+	-	?
4-aminobutanal + NAD+ + H2O	Solanum lycopersicum	-	4-aminobutanoate + NADH + 2 H+	-	?
4-aminobutanal + NAD+ + H2O	Zea mays	-	4-aminobutanoate + NADH + 2 H+	-	?

Organism

Organism	UniProt	Comment	Textmining
Solanum lycopersicum	-	-	-
Solanum lycopersicum	B6ECN9	-	-
Zea mays	C0P9J6	-	-
Zea mays	C6KEM4	-	-
Zea mays	G5DDC2	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
corn silk	-	Zea mays	-
cotyledon	-	Solanum lycopersicum	-
flower	-	Solanum lycopersicum	-
fruit	-	Solanum lycopersicum	-
kernel	-	Zea mays	-
leaf	-	Zea mays	-
additional information	isozyme tissue distribution, overview	Solanum lycopersicum	-
additional information	isozyme tissue distribution, overview	Zea mays	-
petal	-	Solanum lycopersicum	-
root	-	Solanum lycopersicum	-
root	-	Zea mays	-
sepal	-	Solanum lycopersicum	-
shoot apex	-	Solanum lycopersicum	-
stamen	-	Zea mays	-
stem	-	Solanum lycopersicum	-
tassel	-	Zea mays	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
3-aminopropanal + NAD+ + H2O	-	Solanum lycopersicum	3-aminopropanoate + NADH + H+	-	?
3-aminopropanal + NAD+ + H2O	-	Zea mays	3-aminopropanoate + NADH + H+	-	?
3-aminopropanal + NAD+ + H2O	best substrate	Zea mays	3-aminopropanoate + NADH + H+	-	?
3-aminopropanal + NAD+ + H2O	best substrate	Solanum lycopersicum	3-aminopropanoate + NADH + H+	-	?
3-aminopropanal + NAD+ + H2O	high activity	Solanum lycopersicum	3-aminopropanoate + NADH + H+	-	?
3-pyridine carboxaldehyde + NAD+ + H2O	-	Solanum lycopersicum	3-pyridine carboxylic acid + NADH + 2 H+	-	?
4-aminobutanal + NAD+ + H2O	-	Solanum lycopersicum	4-aminobutanoate + NADH + 2 H+	-	?
4-aminobutanal + NAD+ + H2O	-	Zea mays	4-aminobutanoate + NADH + 2 H+	-	?
4-guanidinobutyraldehyde + NAD+ + H2O	-	Solanum lycopersicum	4-guanidinobutanoate + NADH + 2 H+	-	?
4-guanidinobutyraldehyde + NAD+ + H2O	-	Zea mays	4-guanidinobutanoate + NADH + 2 H+	-	?
4-pyridine carboxaldehyde + NAD+ + H2O	-	Solanum lycopersicum	4-pyridine carboxylic acid + NADH + 2 H+	-	?
betaine aldehyde + NAD+ + H2O	-	Solanum lycopersicum	betaine + NADH + 2 H+	-	?
betaine aldehyde + NAD+ + H2O	-	Zea mays	betaine + NADH + 2 H+	-	?
additional information	identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate	Solanum lycopersicum	?	-	?
additional information	identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate. No or poor activity with 3-pyridine carboxaldehyde and 4-pyridine carboxaldehyde	Zea mays	?	-	?
additional information	identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate. No or poor activity with betaine aldehyde, 3-pyridine carboxaldehyde, and 4-pyridine carboxaldehyde	Zea mays	?	-	?
additional information	identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate. No or poor activity with betaine aldehyde, 3-pyridine carboxaldehyde, and 4-pyridine carboxaldehyde	Solanum lycopersicum	?	-	?
N,N,N-trimethyl-4-aminobutyraldehyde + NAD+ + H2O	-	Zea mays	N,N,N-trimethyl-4-aminobutanoate + NADH + 2 H+	-	?
N,N,N-trimethyl-4-aminobutyraldehyde + NAD+ + H2O	-	Solanum lycopersicum	N,N,N-trimethyl-4-aminobutanoate + NADH + 2 H+	-	?
N,N,N-trimethyl-4-aminobutyraldehyde + NAD+ + H2O	best substrate	Solanum lycopersicum	N,N,N-trimethyl-4-aminobutanoate + NADH + 2 H+	-	?
N,N,N-trimethyl-4-aminobutyraldehyde + NAD+ + H2O	best substrate	Zea mays	N,N,N-trimethyl-4-aminobutanoate + NADH + 2 H+	-	?

Subunits

Subunits	Comment	Organism
dimer	plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site	Solanum lycopersicum
dimer	plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site	Zea mays

Synonyms

Synonyms	Comment	Organism
4-aminobutyraldehyde dehydrogenase	-	Solanum lycopersicum
4-aminobutyraldehyde dehydrogenase	-	Zea mays
SlAMADH1	-	Solanum lycopersicum
SlAMADH2	-	Solanum lycopersicum
ZmAMADH1a	-	Zea mays
ZmAMADH1b	-	Zea mays
ZmAMADH2	-	Zea mays

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Solanum lycopersicum
37	-	assay at	Zea mays

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism
0.07	-	Betaine aldehyde	pH 9.0, 37°C	Zea mays
0.6	-	Betaine aldehyde	pH 9.0, 37°C	Zea mays
1	-	Betaine aldehyde	pH 9.0, 37°C	Solanum lycopersicum
1.2	-	4-aminobutanal	pH 9.0, 37°C	Zea mays
1.4	-	4-pyridine carboxaldehyde	pH 9.0, 37°C	Solanum lycopersicum
1.6	-	4-guanidinobutyraldehyde	pH 9.0, 37°C	Zea mays
1.7	-	4-aminobutanal	pH 9.0, 37°C	Zea mays
1.7	-	4-guanidinobutyraldehyde	pH 9.0, 37°C	Zea mays
2	-	N,N,N-trimethyl-4-aminobutyraldehyde	pH 9.0, 37°C	Solanum lycopersicum
2.2	-	3-pyridine carboxaldehyde	pH 9.0, 37°C	Solanum lycopersicum
2.5	-	4-aminobutanal	pH 9.0, 37°C	Solanum lycopersicum
3.6	-	N,N,N-trimethyl-4-aminobutyraldehyde	pH 9.0, 37°C	Solanum lycopersicum
3.9	-	4-guanidinobutyraldehyde	pH 9.0, 37°C	Solanum lycopersicum
4.3	-	4-aminobutanal	pH 9.0, 37°C	Zea mays
4.5	-	4-guanidinobutyraldehyde	pH 9.0, 37°C	Solanum lycopersicum
5	-	4-guanidinobutyraldehyde	pH 9.0, 37°C	Zea mays
5.1	-	N,N,N-trimethyl-4-aminobutyraldehyde	pH 9.0, 37°C	Zea mays
5.2	-	4-aminobutanal	pH 9.0, 37°C	Solanum lycopersicum
5.7	-	N,N,N-trimethyl-4-aminobutyraldehyde	pH 9.0, 37°C	Zea mays
6	-	3-aminopropanal	pH 9.0, 37°C	Solanum lycopersicum
8.2	-	3-aminopropanal	pH 9.0, 37°C	Solanum lycopersicum
10.3	-	3-aminopropanal	pH 9.0, 37°C	Zea mays
10.8	-	N,N,N-trimethyl-4-aminobutyraldehyde	pH 9.0, 37°C	Zea mays
11.1	-	3-aminopropanal	pH 9.0, 37°C	Zea mays
11.8	-	3-aminopropanal	pH 9.0, 37°C	Zea mays

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
9.4	9.8	-	Zea mays
9.4	9.8	-	Solanum lycopersicum
10.2	-	-	Solanum lycopersicum
10.2	-	-	Zea mays

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	binding structure and site	Solanum lycopersicum
NAD+	binding structure and site	Zea mays

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism
0.09	-	N,N,N-trimethyl-4-aminobutyraldehyde	pH 9.0, 37°C	Solanum lycopersicum
0.111	-	3-aminopropanal	pH 9.0, 37°C	Solanum lycopersicum
0.211	-	4-guanidinobutyraldehyde	pH 9.0, 37°C	Solanum lycopersicum
0.581	-	4-guanidinobutyraldehyde	pH 9.0, 37°C	Solanum lycopersicum
0.858	-	4-aminobutanal	pH 9.0, 37°C	Solanum lycopersicum
0.914	-	3-aminopropanal	pH 9.0, 37°C	Solanum lycopersicum
1.56	-	N,N,N-trimethyl-4-aminobutyraldehyde	pH 9.0, 37°C	Solanum lycopersicum

General Information

General Information	Comment	Organism
evolution	the enzyme is a member of the aldehyde dehydrogenase 10 family	Solanum lycopersicum
evolution	the enzyme is a member of the aldehyde dehydrogenase 10 family	Zea mays
additional information	plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site. The catalytic mechanism follows the sequential binding model valid for the ALDH superfamily. Aminoaldehyde substrates undergo a nucleophilic attack by the catalytic cysteine, leading to a thioester formation (i.e. a covalent intermediate) and the subsequent hydride transfer to NAD+. The conserved glutamate residue functions as a general base activating a water molecule. Such a molecule performs a nucleophilic attack at the thioester acyl-sulfur bond, resulting in the release of the amino acid	Solanum lycopersicum
additional information	plant AMADHs are dimeric and possess a 14-A long substrate channel in each monomer. There are three strictly conserved residues essential for the catalysis, Asn162, Cys294, and Glu260, which lie in PWNYP, GQI(V)CSATSR, and ELGGKSP consensus motifs. The three catalytic residues (Asn, Cys, and Glu) lie at the substrate channel bottom and together form the active site. The catalytic mechanism follows the sequential binding model valid for the ALDH superfamily. Aminoaldehyde substrates undergo a nucleophilic attack by the catalytic cysteine, leading to a thioester formation (i.e. a covalent intermediate) and the subsequent hydride transfer to NAD+. The conserved glutamate residue functions as a general base activating a water molecule. Such a molecule performs a nucleophilic attack at the thioester acyl-sulfur bond, resulting in the release of the amino acid	Zea mays

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism
0.46	-	Betaine aldehyde	pH 9.0, 37°C	Solanum lycopersicum
2.3	-	Betaine aldehyde	pH 9.0, 37°C	Zea mays
6.9	-	3-pyridine carboxaldehyde	pH 9.0, 37°C	Solanum lycopersicum
14	-	N,N,N-trimethyl-4-aminobutyraldehyde	pH 9.0, 37°C	Solanum lycopersicum
19	-	4-aminobutanal	pH 9.0, 37°C	Solanum lycopersicum
28	-	4-pyridine carboxaldehyde	pH 9.0, 37°C	Solanum lycopersicum
42	-	4-aminobutanal	pH 9.0, 37°C	Zea mays
45	-	Betaine aldehyde	pH 9.0, 37°C	Zea mays
46	-	4-aminobutanal	pH 9.0, 37°C	Solanum lycopersicum
53	-	4-guanidinobutyraldehyde	pH 9.0, 37°C	Solanum lycopersicum
65	-	4-aminobutanal	pH 9.0, 37°C	Zea mays
72	-	4-aminobutanal	pH 9.0, 37°C	Zea mays
110	-	3-aminopropanal	pH 9.0, 37°C	Zea mays
150	-	3-aminopropanal	pH 9.0, 37°C	Solanum lycopersicum
180	-	4-guanidinobutyraldehyde	pH 9.0, 37°C	Solanum lycopersicum
210	-	N,N,N-trimethyl-4-aminobutyraldehyde	pH 9.0, 37°C	Solanum lycopersicum
350	-	4-guanidinobutyraldehyde	pH 9.0, 37°C	Zea mays
450	-	4-guanidinobutyraldehyde	pH 9.0, 37°C	Zea mays
520	-	4-guanidinobutyraldehyde	pH 9.0, 37°C	Zea mays
570	-	N,N,N-trimethyl-4-aminobutyraldehyde	pH 9.0, 37°C	Zea mays
680	-	N,N,N-trimethyl-4-aminobutyraldehyde	pH 9.0, 37°C	Zea mays
840	-	N,N,N-trimethyl-4-aminobutyraldehyde	pH 9.0, 37°C	Zea mays
910	-	3-aminopropanal	pH 9.0, 37°C	Solanum lycopersicum
1000	-	3-aminopropanal	pH 9.0, 37°C	Zea mays
1300	-	3-aminopropanal	pH 9.0, 37°C	Zea mays