Activating Compound | Comment | Organism | Structure |
---|---|---|---|
pyrroloquinoline quinone | absolutely required for activity, one mole of PQQ is bound to one mole of apoenzyme | Sphingopyxis sp. |
Cloned (Comment) | Organism |
---|---|
gene pvadh, DNA and amino acid sequence determination and analysis, sequence comparison, expression of His6-tagged enzyme in Escherichia coli | Sphingopyxis sp. |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
periplasm | - |
Sphingopyxis sp. | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | high activation | Sphingopyxis sp. | |
Mg2+ | activates, the activation by Mg2+ is less than 80% of the activation by Ca2+ | Sphingopyxis sp. |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
68000 | - |
recombinant enzyme, gel filtration | Sphingopyxis sp. |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sphingopyxis sp. | Q588Z1 | gene pvadh; gene pvadh or pvaA | - |
Purification (Comment) | Organism |
---|---|
recombinant His6-tagged enzyme from Escherichia coli 44fold to homogeneity | Sphingopyxis sp. |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
18 | - |
purified recombinant enzyme, substrate PVA117 | Sphingopyxis sp. |
Storage Stability | Organism |
---|---|
4°C, purified recombinant enzyme, 20 mM Tris/HCl buffer, pH 8.0, stable for more than a month | Sphingopyxis sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1,3-butanediol + O2 | low activity | Sphingopyxis sp. | ? | - |
? | |
2,4-pentanediol + O2 | low activity | Sphingopyxis sp. | ? | - |
? | |
cyclohexanediol + O2 | low activity | Sphingopyxis sp. | ? | - |
? | |
additional information | no activity with primary nor secondary alcohols | Sphingopyxis sp. | ? | - |
? | |
polypropylene glycol + O2 | - |
Sphingopyxis sp. | ? | - |
? | |
polyvinyl alcohol + O2 | substrate PVA117 | Sphingopyxis sp. | oxidized polyvinyl alcohol + H2O2 | - |
? | |
pyrroloquinoline quinone + O2 | low activity | Sphingopyxis sp. | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | 1 * 68000, recombinant enzyme, SDS-PAGE | Sphingopyxis sp. |
More | the enzyme possesses a conserved superbarrel domain SD, probable PQQ-binding amino acids in the SD and a hem-binding domain HBD | Sphingopyxis sp. |
Synonyms | Comment | Organism |
---|---|---|
periplasmic poly(vinyl alcohol) dehydrogenase | - |
Sphingopyxis sp. |
PVA dehydrogenase | - |
Sphingopyxis sp. |
PVADH | - |
Sphingopyxis sp. |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
recombinant enzyme | Sphingopyxis sp. |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.2 | 7.4 | dependent on buffer system, recombinant enzyme | Sphingopyxis sp. |