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Literature summary for 1.1.1.250 extracted from
- Properties of recombinant Strep-tagged and untagged hyperthermophilic D-arabitol dehydrogenase from Thermotoga maritima (2011), Appl. Microbiol. Biotechnol., 90, 1285-1293 .
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | the enzyme catalyzed oxidation of D-arabitol to D-ribulose which is a rare ketopentose sugar that has numerous industrially applications. D-Arabitol 2-dehydrogenase from Thermotoga maritima has the potential to be a useful biocatalyst for the production of D-ribulose starting from the inexpensive D-arabitol due to its regiospecificity and thermostability | Thermotoga maritima |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli | Thermotoga maritima |
General Stability
| General Stability | Organism |
|---|---|
| K+, 60 mM, twofold increase in catalytic rates. K+ likely contributes to the overall stability of the protein and is not required for catalytic activity | Thermotoga maritima |
| Mg2+, 55 mM, twofold increase in catalytic rates. Mg2+ likely contributes to the overall stability of the protein and is not required for catalytic activity | Thermotoga maritima |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.027 | - |
NADH | 85°C, pH 7.5, Strep-tagged enzyme, cosubstrate D-ribulose | Thermotoga maritima |  |
| 0.031 | - |
NADH | 85°C, pH 7.5, tag-less enzyme, cosubstrate D-ribulose | Thermotoga maritima | |
| 0.059 | - |
NAD+ | 85°C, pH 8.5, tag-less enzyme, cosubstrate D-arabitol | Thermotoga maritima | |
| 0.069 | - |
NAD+ | 85°C, pH 8.5, Strep-tagged enzyme, cosubstrate D-arabitol | Thermotoga maritima | |
| 2.6 | - |
D-arabitol | 85°C, pH 8.5, tag-less enzyme | Thermotoga maritima | |
| 7.1 | - |
D-arabitol | 85°C, pH 8.5, Strep-tagged enzyme | Thermotoga maritima | |
| 7.2 | - |
D-ribulose | 85°C, pH 7.5, tag-less enzyme | Thermotoga maritima | |
| 13.9 | - |
D-ribulose | 85°C, pH 7.5, Strep-tagged enzyme | Thermotoga maritima | |
| 20 | - |
D-xylitol | 85°C, pH 8.5, Strep-tagged enzyme | Thermotoga maritima | |
| 21.7 | - |
D-xylitol | 85°C, pH 8.5, tag-less enzyme | Thermotoga maritima | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| K+ | 60 mM, twofold increase in catalytic rates. K+ likely contributes to the overall stability of the protein and is not required for catalytic activity | Thermotoga maritima | |
| Mg2+ | 55 mM, twofold increase in catalytic rates. Mg2+ likely contributes to the overall stability of the protein and is not required for catalytic activity | Thermotoga maritima | |
| additional information | no effect on the activity is observed with CaCl2 or NaCl addition, up to 150 mM | Thermotoga maritima |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 164000 | - |
non-denaturing PAGE | Thermotoga maritima |
| 320000 | - |
non-denaturing PAGE | Thermotoga maritima |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermotoga maritima | Q9WYD3 | - |
- |
| Thermotoga maritima DSM 3109 | Q9WYD3 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| purified from Escherichia coli with and without a Strep-tag. The tag-less form of D-arabitol dehydrogenase has similar kinetic parameters compared to the tagged enzyme, demonstrating that the Strep-tag is not deleterious to protein function but decreases protein stability | Thermotoga maritima |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-arabitol + NAD+ | - |
Thermotoga maritima | D-ribulose + NADH + H+ | - |
? | |
| D-arabitol + NAD+ | - |
Thermotoga maritima DSM 3109 | D-ribulose + NADH + H+ | - |
? | |
| D-ribulose + NADH + H+ | - |
Thermotoga maritima | D-arabitol + NAD+ | - |
? | |
| D-ribulose + NADH + H+ | - |
Thermotoga maritima DSM 3109 | D-arabitol + NAD+ | - |
? | |
| D-xylitol + NAD+ | - |
Thermotoga maritima | D-xylulose + NADH + H+ | - |
? | |
| D-xylitol + NAD+ | - |
Thermotoga maritima DSM 3109 | D-xylulose + NADH + H+ | - |
? | |
| D-xylulose + NADH + H+ | - |
Thermotoga maritima | D-xylitol + NAD+ | - |
? | |
| D-xylulose + NADH + H+ | - |
Thermotoga maritima DSM 3109 | D-xylitol + NAD+ | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homododecamer | 12 * 27600, SDS-PAGE | Thermotoga maritima |
| homohexamer | 6 * 27600, SDS-PAGE | Thermotoga maritima |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| D-arabitol 2-dehydrogenase | - |
Thermotoga maritima |
| TM_0297 | - |
Thermotoga maritima |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 85 | - |
substrate: D-arabitol | Thermotoga maritima |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
inactive at temperatures lower than 50 °C | Thermotoga maritima |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 85 | - |
the tag-less protein is thermostable, retaining 90% of its activity after 90 min. The Strep-tagged enzyme loese 60% of its activity after 10 min | Thermotoga maritima |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 11 | - |
D-arabitol | 85°C, pH 8.5, Strep-tagged enzyme | Thermotoga maritima | |
| 11.2 | - |
D-xylitol | 85°C, pH 8.5, Strep-tagged enzyme | Thermotoga maritima | |
| 16.6 | - |
D-xylitol | 85°C, pH 8.5, tag-less enzyme | Thermotoga maritima | |
| 18.7 | - |
D-arabitol | 85°C, pH 8.5, tag-less enzyme | Thermotoga maritima | |
| 165.6 | - |
D-ribulose | 85°C, pH 7.5, Strep-tagged enzyme | Thermotoga maritima | |
| 193.2 | - |
D-ribulose | 85°C, pH 7.5, tag-less enzyme | Thermotoga maritima | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
reduction of D-ribulose | Thermotoga maritima |
| 8.5 | - |
oxidation of D-arabitol | Thermotoga maritima |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4.5 | 9.5 | oxidation of D-arabitol is not observed below pH 4.5 or above pH 9.5 | Thermotoga maritima |
| 5.5 | 8.5 | pH 5.5: about 40% of maximal activity, pH 8.5: about 10% of maximal activity, reduction of D-ribulose | Thermotoga maritima |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | no activity with NADP+ | Thermotoga maritima | |
| NADH | no activity with NADPH | Thermotoga maritima | |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.56 | - |
D-xylitol | 85°C, pH 8.5, Strep-tagged enzyme | Thermotoga maritima | |
| 0.74 | - |
D-xylitol | 85°C, pH 8.5, tag-less enzyme | Thermotoga maritima | |
| 1.5 | - |
D-arabitol | 85°C, pH 8.5, Strep-tagged enzyme | Thermotoga maritima | |
| 7.2 | - |
D-arabitol | 85°C, pH 8.5, tag-less enzyme | Thermotoga maritima | |
| 12 | - |
D-ribulose | 85°C, pH 7.5, Strep-tagged enzyme | Thermotoga maritima | |
| 27 | - |
D-ribulose | 85°C, pH 7.5, tag-less enzyme | Thermotoga maritima | |
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