EC Number | Application | Comment | Organism |
---|---|---|---|
1.1.1.6 | biotechnology | GlyDH is active with immobilized N6-CM-NAD+, suggesting that N6-CM-NAD+ can be immobilized on an electrode to allow TmGlyDH activity in a system that reoxidizes the cofactor electrocatalytically, development of a bioelectrocatalytic reactor | Thermotoga maritima |
1.1.1.6 | synthesis | GlyDH is active with immobilized N6-CM-NAD+, suggesting that N6-CM-NAD+ can be immobilized on an electrode to allow TmGlyDH activity in a system that reoxidizes the cofactor electrocatalytically, development of a bioelectrocatalytic reactor | Thermotoga maritima |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.1.6 | gene gldA, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Thermotoga maritima |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.1.1.6 | I154A | site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme | Thermotoga maritima |
1.1.1.6 | I154A/K157G | site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme | Thermotoga maritima |
1.1.1.6 | I154A/K157N | site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme | Thermotoga maritima |
1.1.1.6 | K157G | site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme | Thermotoga maritima |
1.1.1.6 | K157N | site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme | Thermotoga maritima |
1.1.1.6 | V44A | site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme | Thermotoga maritima |
1.1.1.6 | V44A/I154A | site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme | Thermotoga maritima |
1.1.1.6 | V44A/K157G | site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme | Thermotoga maritima |
1.1.1.6 | V44A/K157G | site-directed mutagenesis, wild-type enzyme TmGlyDH shows little activity with N6-carboxymethyl-NAD+ (N6-CM-NAD), an NAD+ analogue modified for easy immobilization to amino groups, but the double mutation V44A/K157G increases catalytic efficiency with N6-CMNAD+ by 10fold | Thermotoga maritima |
1.1.1.6 | V44A/K157N | site-directed mutagenesis, the mutant shows altered activity with cofactor derivative N6-CM-NAD+ immobilized on Sepharose beads compared to the wild-type enzyme | Thermotoga maritima |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.1.1.6 | additional information | - |
additional information | Michaelis-Menten kinetics, cooperative behavior of TmGlyDH | Thermotoga maritima | |
1.1.1.6 | 0.02 | - |
NADH | pH 7.9, 50°C, recombinant wild-type enzyme | Thermotoga maritima | |
1.1.1.6 | 0.021 | - |
NAD+ | pH 7.4, 50°C, recombinant mutant V44A/K157G | Thermotoga maritima | |
1.1.1.6 | 0.024 | - |
NAD+ | pH 7.4, 50°C, recombinant wild-type enzyme | Thermotoga maritima | |
1.1.1.6 | 0.025 | - |
NAD+ | pH 7.4, 50°C, recombinant mutant K157N | Thermotoga maritima | |
1.1.1.6 | 0.031 | - |
NAD+ | pH 7.4, 50°C, recombinant mutant K157G | Thermotoga maritima | |
1.1.1.6 | 0.039 | - |
NAD+ | pH 7.4, 50°C, recombinant mutant V44A/K157N | Thermotoga maritima | |
1.1.1.6 | 0.051 | - |
NAD+ | pH 7.9, 50°C, recombinant wild-type enzyme | Thermotoga maritima | |
1.1.1.6 | 0.07 | - |
NAD+ | pH 7.4, 50°C, recombinant mutant V44A | Thermotoga maritima | |
1.1.1.6 | 0.08 | - |
N6-carboxymethyl-NAD+ | pH 7.4, 50°C, recombinant mutant K157G | Thermotoga maritima | |
1.1.1.6 | 0.08 | - |
N6-carboxymethyl-NAD+ | mutant enzyme K157G, at pH 7.4 and 50°C | Thermotoga maritima | |
1.1.1.6 | 0.088 | - |
NAD+ | pH 7.4, 50°C, recombinant mutant I154A | Thermotoga maritima | |
1.1.1.6 | 0.108 | - |
NAD+ | pH 7.4, 50°C, recombinant mutant I154A/K157G | Thermotoga maritima | |
1.1.1.6 | 0.15 | - |
N6-carboxymethyl-NAD+ | pH 7.4, 50°C, recombinant mutant V44A | Thermotoga maritima | |
1.1.1.6 | 0.15 | - |
N6-carboxymethyl-NAD+ | mutant enzyme V44A, at pH 7.4 and 50°C | Thermotoga maritima | |
1.1.1.6 | 0.186 | - |
N6-carboxymethyl-NAD+ | pH 7.4, 50°C, recombinant mutant V44A/K157N | Thermotoga maritima | |
1.1.1.6 | 0.186 | - |
N6-carboxymethyl-NAD+ | mutant enzyme V44A/ K157N, at pH 7.4 and 50°C | Thermotoga maritima | |
1.1.1.6 | 0.25 | - |
N6-carboxymethyl-NAD+ | pH 7.4, 50°C, recombinant mutant V44A/K157G | Thermotoga maritima | |
1.1.1.6 | 0.25 | - |
N6-carboxymethyl-NAD+ | mutant enzyme V44A/K157G, at pH 7.4 and 50°C | Thermotoga maritima | |
1.1.1.6 | 0.351 | - |
NAD+ | pH 7.4, 50°C, recombinant mutant V44A/I154A | Thermotoga maritima | |
1.1.1.6 | 0.36 | - |
N6-carboxymethyl-NAD+ | pH 7.4, 50°C, recombinant mutant K157N | Thermotoga maritima | |
1.1.1.6 | 0.36 | - |
N6-carboxymethyl-NAD+ | mutant enzyme K157N, at pH 7.4 and 50°C | Thermotoga maritima | |
1.1.1.6 | 0.37 | - |
N6-carboxymethyl-NAD+ | pH 7.4, 50°C, recombinant wild-type enzyme | Thermotoga maritima | |
1.1.1.6 | 0.37 | - |
N6-carboxymethyl-NAD+ | wild type enzyme, at pH 7.4 and 50°C | Thermotoga maritima | |
1.1.1.6 | 0.6 | - |
NAD+ | pH 7.4, 50°C, recombinant mutant V44A/I154A/K157G | Thermotoga maritima | |
1.1.1.6 | 0.73 | - |
N6-carboxymethyl-NAD+ | pH 7.4, 50°C, recombinant mutant I154A | Thermotoga maritima | |
1.1.1.6 | 0.73 | - |
N6-carboxymethyl-NAD+ | mutant enzyme I154A, at pH 7.4 and 50°C | Thermotoga maritima | |
1.1.1.6 | 1.5 | - |
N6-carboxymethyl-NAD+ | pH 7.4, 50°C, recombinant mutant I154A/K157G | Thermotoga maritima | |
1.1.1.6 | 1.5 | - |
N6-carboxymethyl-NAD+ | mutant enzyme I154A/K157G, at pH 7.4 and 50°C | Thermotoga maritima | |
1.1.1.6 | 2.3 | - |
N6-carboxymethyl-NAD+ | pH 7.4, 50°C, recombinant mutant V44A/I154A/K157G | Thermotoga maritima | |
1.1.1.6 | 2.3 | - |
N6-carboxymethyl-NAD+ | mutant enzyme V44A/I154A/K157G, at pH 7.4 and 50°C | Thermotoga maritima | |
1.1.1.6 | 2.9 | - |
N6-carboxymethyl-NAD+ | pH 7.4, 50°C, recombinant mutant V44A/I154A | Thermotoga maritima | |
1.1.1.6 | 2.9 | - |
N6-carboxymethyl-NAD+ | mutant enzyme V44A/ I154A, at pH 7.4 and 50°C | Thermotoga maritima |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.6 | glycerol + NAD+ | Thermotoga maritima | - |
glycerone + NADH + H+ | - |
r | |
1.1.1.6 | glycerol + NAD+ | Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 | - |
glycerone + NADH + H+ | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.6 | Thermotoga maritima | Q9WYQ4 | - |
- |
1.1.1.6 | Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 | Q9WYQ4 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.1.1.6 | gene gldA, recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, and dialysis | Thermotoga maritima |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.1.1.6 | 45 | - |
purified recombinant enzyme, oxidation of glycerol, 80°C, pH 7.4 | Thermotoga maritima |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.1.1.6 | (R)-1,2-propanediol + NAD+ | the enzyme prefers the R-enantiomer | Thermotoga maritima | hydroxyacetone + NADH | - |
r | |
1.1.1.6 | (R)-1,2-propanediol + NAD+ | the enzyme prefers the R-enantiomer | Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 | hydroxyacetone + NADH | - |
r | |
1.1.1.6 | 1,2-butanediol + NAD+ | - |
Thermotoga maritima | ? + NADH | - |
? | |
1.1.1.6 | 1,2-butanediol + NAD+ | - |
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 | ? + NADH | - |
? | |
1.1.1.6 | glycerol + N6-carboxymethyl-NAD+ | - |
Thermotoga maritima | glycerone + N6-carboxymethyl-NADH + H+ | - |
r | |
1.1.1.6 | glycerol + N6-carboxymethyl-NAD+ | - |
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 | glycerone + N6-carboxymethyl-NADH + H+ | - |
r | |
1.1.1.6 | glycerol + N6-CM-NAD+ | - |
Thermotoga maritima | glycerone + N6-carboxymethyl-NADH + H+ | - |
r | |
1.1.1.6 | glycerol + N6-CM-NAD+ | - |
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 | glycerone + N6-carboxymethyl-NADH + H+ | - |
r | |
1.1.1.6 | glycerol + NAD+ | - |
Thermotoga maritima | glycerone + NADH + H+ | - |
r | |
1.1.1.6 | glycerol + NAD+ | - |
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 | glycerone + NADH + H+ | - |
r |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.6 | GldA | - |
Thermotoga maritima |
1.1.1.6 | TmGlyDH | - |
Thermotoga maritima |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.1.1.6 | 80 | - |
assay at | Thermotoga maritima |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.1.1.6 | 90 | - |
reduction activity | Thermotoga maritima |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.1.1.6 | 50 | - |
the recombinant enzyme is initially more stable in the presence of DHA than in its absence, maintaining 100% activity over 120 min, but it quickly inactivates after 120 min, losing over 84% of its activity in the next 5 h | Thermotoga maritima |
1.1.1.6 | 80 | - |
the recombinant enzyme, 40% activity remaining after 25 min, 20% activity remaining after 150 min | Thermotoga maritima |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.1.1.6 | 7.9 | - |
- |
Thermotoga maritima |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
1.1.1.6 | 6 | 8.5 | oxidation activity range | Thermotoga maritima |
1.1.1.6 | 6.4 | 9 | reduction activity range | Thermotoga maritima |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.1.6 | N6-carboxymethyl-NAD+ | wild-type enzyme TmGlyDH shows little activity with N6-carboxymethyl-NAD+ (N6-CM-NAD), an NAD+ analogue modified for easy immobilization to amino groups, but the double mutation V44A/K157G increases catalytic efficiency with N6-CMNAD+ by 10fold. kinetics with N6-CM-NAD+ and modelling, overview. N6-CM-NAD+ is immobilized on cyanogen bromide-activated Sepharose 4b | Thermotoga maritima | |
1.1.1.6 | NAD+ | - |
Thermotoga maritima | |
1.1.1.6 | NADH | - |
Thermotoga maritima |