Protein Variants | Comment | Organism |
---|---|---|
F412I/W561Q | wild-type enzyme shows no activity with 5-(hydroxymethyl)furfural, mutant enzyme shows low activity (0.35 U/mg) | Pseudomonas putida |
F412I/W561S | wild-type enzyme shows no activity with 5-(hydroxymethyl)furfural, mutant enzyme shows low activity (0.12 U/mg) | Pseudomonas putida |
F412V/W561A | wild-type enzyme shows no activity with 5-(hydroxymethyl)furfural, mutant enzyme shows activity (1.04 U/mg). The mutant enzyma slso The KM-value for ethanol is approximately 525fold higher than that the wild-type value, whereas the maximal velocity is unchanged. This suggests that the oxidative capability of the PedHF412V/W561A variant is unaffected by the amino acid changes, and only the substrate binding is modulated | Pseudomonas putida |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.016 | - |
ethanol | wild-type enzyme, pH and temperature not specified in the publication | Pseudomonas putida | |
2.3 | - |
5-formylfurfural | mutant enzyme F412V/W561A, pH and temperature not specified in the publication | Pseudomonas putida | |
8.4 | - |
ethanol | mutant enzyme F412V/W561A, pH and temperature not specified in the publication | Pseudomonas putida | |
13.3 | - |
5-(hydroxymethyl)furfural | mutant enzyme F412V/W561A, pH and temperature not specified in the publication | Pseudomonas putida | |
18.8 | - |
5-(hydroxymethyl)furoic acid | mutant enzyme F412V/W561A, pH and temperature not specified in the publication | Pseudomonas putida |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
periplasm | - |
Pseudomonas putida | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas putida | Q88JH0 | - |
- |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.12 | - |
substrate: 5-(hydroxymethyl)furoic acid, mutant enzyme F412I/W561S, pH and temperature not specified in the publication | Pseudomonas putida |
0.35 | - |
substrate: 5-(hydroxymethyl)furoic acid, mutant enzyme F412I/W561Q, pH and temperature not specified in the publication | Pseudomonas putida |
1.04 | - |
substrate: 5-(hydroxymethyl)furoic acid, mutant enzyme F412V/W561A, pH and temperature not specified in the publication | Pseudomonas putida |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
5-(hydroxymethyl)furfural + phenazine methosulfate | - |
Pseudomonas putida | ? + reduced phenazine methosulfate | - |
? | |
5-(hydroxymethyl)furoic acid + phenazine methosulfate | wild-type enzyme shows no activity, mutant enzymes F412V/W561A, F412I/W561Q and F412I/W561S are active | Pseudomonas putida | ? + reduced phenazine methosulfate | - |
? | |
5-formylfurfural + phenazine methosulfate | - |
Pseudomonas putida | ? + reduced phenazine methosulfate | - |
? | |
ethanol + phenazine methosulfate | - |
Pseudomonas putida | acetaldehyde + reduced phenazine methosulfate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
PedH | - |
Pseudomonas putida |
pyrroloquinoline quinone (PQQ)-dependent alcohol dehydrogenase | - |
Pseudomonas putida |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.2 | - |
5-(hydroxymethyl)furoic acid | mutant enzyme F412V/W561A, pH and temperature not specified in the publication | Pseudomonas putida | |
4.1 | - |
5-formylfurfural | mutant enzyme F412V/W561A, pH and temperature not specified in the publication | Pseudomonas putida | |
5 | - |
ethanol | wild-type enzyme, pH and temperature not specified in the publication | Pseudomonas putida | |
5.1 | - |
ethanol | mutant enzyme F412V/W561A, pH and temperature not specified in the publication | Pseudomonas putida | |
5.1 | - |
5-(hydroxymethyl)furfural | mutant enzyme F412V/W561A, pH and temperature not specified in the publication | Pseudomonas putida |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyrroloquinoline quinone | pyrroloquinoline quinone-dependent dehydrogenase, pyrroloquinoline quinone is coordinated by Q87, I135, R137, S181, R350, L413, N417, W418, and W493. The side chains of W263 and the vicinal disulfide bond between C131 and C132 provide additional stacking interactions | Pseudomonas putida |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.06 | - |
5-(hydroxymethyl)furoic acid | mutant enzyme F412V/W561A, pH and temperature not specified in the publication | Pseudomonas putida | |
0.38 | - |
5-(hydroxymethyl)furfural | mutant enzyme F412V/W561A, pH and temperature not specified in the publication | Pseudomonas putida | |
0.6 | - |
ethanol | mutant enzyme F412V/W561A, pH and temperature not specified in the publication | Pseudomonas putida | |
1.81 | - |
5-formylfurfural | mutant enzyme F412V/W561A, pH and temperature not specified in the publication | Pseudomonas putida | |
312 | - |
ethanol | wild-type enzyme, pH and temperature not specified in the publication | Pseudomonas putida |