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Literature summary for 1.2.1.3 extracted from

  • Liu, T.; Hao, L.; Wang, R.; Liu, B.
    Molecular characterization of a thermostable aldehyde dehydrogenase (ALDH) from the hyperthermophilic archaeon Sulfolobus tokodaii strain 7 (2013), Extremophiles, 17, 181-190.
    View publication on PubMed
Search for more literature for 1.2.1.3

Activating Compound

Activating Compound Comment Organism Structure
2-mercaptoethanol about 140% activity at 5 mM Sulfurisphaera tokodaii
dithiothreitol about 150% activity at 5 mM Sulfurisphaera tokodaii

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL cells Sulfurisphaera tokodaii

Protein Variants

Protein Variants Comment Organism
C274A the mutation leads to a drastic loss of the activity Sulfurisphaera tokodaii
C274S the mutation leads to a drastic loss of the activity Sulfurisphaera tokodaii
E240A the mutation leads to a drastic loss of the activity Sulfurisphaera tokodaii
E240S the mutation leads to a drastic loss of the activity Sulfurisphaera tokodaii
E370Q the mutation results in decreased activity (higher Km and lower kcat values toward NAD+ and acetaldehyde than the wild type enzyme) Sulfurisphaera tokodaii
I168A the mutation results in no obvious change of kinetics properties toward acetaldehyde and a comparable increase of affinity toward NAD+ Sulfurisphaera tokodaii
K165Q the mutation results in decreased activity (higher Km and lower kcat values toward NAD+ and acetaldehyde than the wild type enzyme) Sulfurisphaera tokodaii
N142A the mutation results in decreased activity (higher Km and lower kcat values toward NAD+ and acetaldehyde than the wild type enzyme) Sulfurisphaera tokodaii

Inhibitors

Inhibitors Comment Organism Structure
H2O2
-
 Sulfurisphaera tokodaii
nitroglycerin more than half of the original activity retained in the presence of 5.5 mM and approximate 80% of the activity is lost by the addition of 11 mM nitroglycerin Sulfurisphaera tokodaii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.82
-
 NAD+ with Dl-glyceraldehyde as cosubstrate, in 50 mM Tris/HCl, at pH 8.0 and 80°C Sulfurisphaera tokodaii
0.84
-
 NAD+ with acetaldehyde as cosubstrate, in 50 mM Tris/HCl, at pH 8.0 and 80°C Sulfurisphaera tokodaii
3.81
-
 NADP+ with acetaldehyde as cosubstrate, in 50 mM Tris/HCl, at pH 8.0 and 80°C Sulfurisphaera tokodaii
6.12
-
 DL-glyceraldehyde 3-phosphate in 50 mM Tris/HCl, at pH 8.0 and 80°C Sulfurisphaera tokodaii
6.38
-
 acetaldehyde in 50 mM Tris/HCl, at pH 8.0 and 80°C Sulfurisphaera tokodaii
8.47
-
 NADP+ with Dl-glyceraldehyde as cosubstrate, in 50 mM Tris/HCl, at pH 8.0 and 80°C Sulfurisphaera tokodaii
8.51
-
 DL-glyceraldehyde in 50 mM Tris/HCl, at pH 8.0 and 80°C Sulfurisphaera tokodaii

Metals/Ions

Metals/Ions Comment Organism Structure
K+ 130% activity at 20 mM Sulfurisphaera tokodaii
Li+ 119% activity at 20 mM Sulfurisphaera tokodaii
additional information the enzyme is not influenced by 20 mM Mg2, Cu2+, Ca2+, Ba2+, Ni2+, Co2+, and Sr2+ Sulfurisphaera tokodaii
Na+ 122% activity at 20 mM Sulfurisphaera tokodaii
NH4+ 131% activity at 20 mM Sulfurisphaera tokodaii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
 4 * 50000, SDS-PAGE Sulfurisphaera tokodaii
51300
-
 4 * 51300, calculated from amino acid sequence Sulfurisphaera tokodaii
200000
-
 gel filtration Sulfurisphaera tokodaii

Organic Solvent Stability

Organic Solvent Comment Organism
dithiothreitol the enzyme is stable in dithiothreitol (90% of the original activity remaining) Sulfurisphaera tokodaii
Ethanol the enzyme is stable in ethanol (90% of the original activity remaining) Sulfurisphaera tokodaii
isopropanol the enzyme is stable in isopropanol (90% of the original activity remaining) Sulfurisphaera tokodaii
Methanol the enzyme is stable in methanol (90% of the original activity remaining) Sulfurisphaera tokodaii
phenylmethylsulfonyl fluoride the enzyme is stable in phenylmethylsulfonyl fluoride (90% of the original activity remaining) Sulfurisphaera tokodaii
SDS the enzyme is stable in SDS (90% of the original activity remaining) Sulfurisphaera tokodaii

Organism

Organism UniProt Comment Textmining
Sulfurisphaera tokodaii
-
-
-
Sulfurisphaera tokodaii 7
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA affinity column chromatography Sulfurisphaera tokodaii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,3-dihydroxyacetone + NAD+ + H2O 53.93% activity compared to acetaldehyde Sulfurisphaera tokodaii ? + NADH + H+
-
 ?
3-nitrobenzaldehyde + NAD+ + H2O 32.98% activity compared to acetaldehyde Sulfurisphaera tokodaii 3-nitrobenzoate + NADH + H+
-
 ?
acetaldehyde + NAD+ + H2O 100% activity with acetaldehyde and NAD+ Sulfurisphaera tokodaii acetate + NADH + H+
-
 ?
acetaldehyde + NAD+ + H2O 100% activity with acetaldehyde and NAD+ Sulfurisphaera tokodaii 7 acetate + NADH + H+
-
 ?
acetaldehyde + NADP+ + H2O low activity with NADP+ Sulfurisphaera tokodaii acetate + NADPH + H+
-
 ?
benzaldehyde + NAD+ + H2O 35.5% activity compared to acetaldehyde Sulfurisphaera tokodaii benzoate + NADH + H+
-
 ?
benzaldehyde + NAD+ + H2O 35.5% activity compared to acetaldehyde Sulfurisphaera tokodaii 7 benzoate + NADH + H+
-
 ?
butyraldehyde + NAD+ + H2O 48.15% activity compared to acetaldehyde Sulfurisphaera tokodaii butyrate + NADH + H+
-
 ?
butyraldehyde + NAD+ + H2O 48.15% activity compared to acetaldehyde Sulfurisphaera tokodaii 7 butyrate + NADH + H+
-
 ?
chloral + NAD+ + H2O 2.67% activity compared to acetaldehyde Sulfurisphaera tokodaii trichloroacetate + NADH + H+
-
 ?
D-glyceraldehyde + NAD+ + H2O 50.25% activity compared to acetaldehyde Sulfurisphaera tokodaii D-glycerate + NADH + H+
-
 ?
DL-glyceraldehyde + NAD+ + H2O 77.27% activity compared to acetaldehyde Sulfurisphaera tokodaii DL-glycerate + NADH + H+
-
 ?
DL-glyceraldehyde + NAD+ + H2O low activity with NADP+ Sulfurisphaera tokodaii DL-glycerate + NADH + H+
-
 ?
DL-glyceraldehyde 3-phosphate + NAD+ + H2O 52.7% activity compared to acetaldehyde Sulfurisphaera tokodaii DL-glycerate 3-phosphate + NADH + H+
-
 ?
formaldehyde + NAD+ + H2O 7.77% activity compared to acetaldehyde Sulfurisphaera tokodaii formate + NADH + H+
-
 ?
glycolaldehyde + NAD+ + H2O 75.43% activity compared to acetaldehyde Sulfurisphaera tokodaii glycolate + NADH + H+
-
 ?
additional information no activity with methanol, ethanol and isopropanol Sulfurisphaera tokodaii ?
-
 ?
additional information no activity with methanol, ethanol and isopropanol Sulfurisphaera tokodaii 7 ?
-
 ?
phenylacetaldehyde + NAD+ + H2O 4.21% activity compared to acetaldehyde Sulfurisphaera tokodaii phenylacetate + NADH + H+
-
 ?
propionaldehyde + NAD+ + H2O 56.22% activity compared to acetaldehyde Sulfurisphaera tokodaii propionate + NADH + H+
-
 ?
propionaldehyde + NAD+ + H2O 56.22% activity compared to acetaldehyde Sulfurisphaera tokodaii 7 propionate + NADH + H+
-
 ?

Subunits

Subunits Comment Organism
homotetramer 4 * 50000, SDS-PAGE Sulfurisphaera tokodaii
homotetramer 4 * 51300, calculated from amino acid sequence Sulfurisphaera tokodaii

Synonyms

Synonyms Comment Organism
ALDH
-
 Sulfurisphaera tokodaii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
80
-
-
 Sulfurisphaera tokodaii

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
70 90 about 50% activity at 70°C, 100% activity at 80°C, about 80% activity at 90°C Sulfurisphaera tokodaii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70 90 the enzyme shows no obvious loss of activity after heat-treatment at 70°C for 12 h, and more than 60% of the original activity remains after treatment at 80°C for 12 h. The half-life at 90°C is 4 h Sulfurisphaera tokodaii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.6
-
 NAD+ with DL-glyceraldehyde as cosubstrate, in 50 mM Tris/HCl, at pH 8.0 and 80°C Sulfurisphaera tokodaii
0.83
-
 DL-glyceraldehyde 3-phosphate in 50 mM Tris/HCl, at pH 8.0 and 80°C Sulfurisphaera tokodaii
0.92
-
 DL-glyceraldehyde in 50 mM Tris/HCl, at pH 8.0 and 80°C Sulfurisphaera tokodaii
1.14
-
 acetaldehyde in 50 mM Tris/HCl, at pH 8.0 and 80°C Sulfurisphaera tokodaii
1.63
-
 NADP+ with DL-glyceraldehyde as cosubstrate, in 50 mM Tris/HCl, at pH 8.0 and 80°C Sulfurisphaera tokodaii
2.05
-
 NAD+ with acetaldehyde as cosubstrate, in 50 mM Tris/HCl, at pH 8.0 and 80°C Sulfurisphaera tokodaii
3.71
-
 NADP+ with acetaldehyde as cosubstrate, in 50 mM Tris/HCl, at pH 8.0 and 80°C Sulfurisphaera tokodaii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Sulfurisphaera tokodaii

pH Range

pH Minimum pH Maximum Comment Organism
6 9 about 60% activity at pH 6.0, about 70% activity at pH 7.0, 100% activity pH 8.0, about 85% activity at pH 9.0 Sulfurisphaera tokodaii

Cofactor

Cofactor Comment Organism Structure
NAD+ the enzyme can utilize both NAD+ and NADP+ as cofactors and shows a preference toward NAD+ Sulfurisphaera tokodaii
NADP+ the enzyme can utilize both NAD+ and NADP+ as cofactors and shows a preference toward NAD+ Sulfurisphaera tokodaii

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.11
-
 DL-glyceraldehyde in 50 mM Tris/HCl, at pH 8.0 and 80°C Sulfurisphaera tokodaii
0.14
-
 DL-glyceraldehyde 3-phosphate in 50 mM Tris/HCl, at pH 8.0 and 80°C Sulfurisphaera tokodaii
0.18
-
 acetaldehyde in 50 mM Tris/HCl, at pH 8.0 and 80°C Sulfurisphaera tokodaii
0.19
-
 NADP+ with DL-glyceraldehyde as cosubstrate, in 50 mM Tris/HCl, at pH 8.0 and 80°C Sulfurisphaera tokodaii
0.73
-
 NAD+ with DL-glyceraldehyde as cosubstrate, in 50 mM Tris/HCl, at pH 8.0 and 80°C Sulfurisphaera tokodaii
0.98
-
 NADP+ with acetaldehyde as cosubstrate, in 50 mM Tris/HCl, at pH 8.0 and 80°C Sulfurisphaera tokodaii
2.45
-
 NAD+ with acetaldehyde as cosubstrate, in 50 mM Tris/HCl, at pH 8.0 and 80°C Sulfurisphaera tokodaii