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Literature summary extracted from

  • Wehrmann, M.; Elsayed, E.; Köbbing, S.; Bendz, L.; Lepak, A.; Schwabe, J.; Wierckx, N.; Bange, G.; Klebensberger, J.
    Engineered PQQ-dependent alcohol dehydrogenase for the oxidation of 5-(hydroxymethyl)furoic acid (2020), ACS Catal., 10, 7836-7842 .
No PubMed abstract available

Protein Variants

EC Number Protein Variants Comment Organism
1.1.5.5 F412I/W561Q wild-type enzyme shows no activity with 5-(hydroxymethyl)furfural, mutant enzyme shows low activity (0.35 U/mg) Pseudomonas putida
1.1.5.5 F412I/W561S wild-type enzyme shows no activity with 5-(hydroxymethyl)furfural, mutant enzyme shows low activity (0.12 U/mg) Pseudomonas putida
1.1.5.5 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.5.5 0.016
-
 ethanol wild-type enzyme, pH and temperature not specified in the publication Pseudomonas putida
1.1.5.5 2.3
-
 5-formylfurfural mutant enzyme F412V/W561A, pH and temperature not specified in the publication Pseudomonas putida
1.1.5.5 8.4
-
 ethanol mutant enzyme F412V/W561A, pH and temperature not specified in the publication Pseudomonas putida
1.1.5.5 13.3
-
 5-(hydroxymethyl)furfural mutant enzyme F412V/W561A, pH and temperature not specified in the publication Pseudomonas putida
1.1.5.5 18.8
-
 5-(hydroxymethyl)furoic acid mutant enzyme F412V/W561A, pH and temperature not specified in the publication Pseudomonas putida

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.5.5 periplasm
-
 Pseudomonas putida
-
-

Organism

EC Number Organism UniProt Comment Textmining
1.1.5.5 Pseudomonas putida Q88JH0
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.5.5 0.12
-
 substrate: 5-(hydroxymethyl)furoic acid, mutant enzyme F412I/W561S, pH and temperature not specified in the publication Pseudomonas putida
1.1.5.5 0.35
-
 substrate: 5-(hydroxymethyl)furoic acid, mutant enzyme F412I/W561Q, pH and temperature not specified in the publication Pseudomonas putida
1.1.5.5 1.04
-
 substrate: 5-(hydroxymethyl)furoic acid, mutant enzyme F412V/W561A, pH and temperature not specified in the publication Pseudomonas putida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.5.5 5-(hydroxymethyl)furfural + phenazine methosulfate
-
 Pseudomonas putida ? + reduced phenazine methosulfate
-
 ?
1.1.5.5 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
-
 ?
1.1.5.5 5-formylfurfural + phenazine methosulfate
-
 Pseudomonas putida ? + reduced phenazine methosulfate
-
 ?
1.1.5.5 ethanol + phenazine methosulfate
-
 Pseudomonas putida acetaldehyde + reduced phenazine methosulfate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.5.5 PedH
-
 Pseudomonas putida
1.1.5.5 pyrroloquinoline quinone (PQQ)-dependent alcohol dehydrogenase
-
 Pseudomonas putida

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.5.5 1.2
-
 5-(hydroxymethyl)furoic acid mutant enzyme F412V/W561A, pH and temperature not specified in the publication Pseudomonas putida
1.1.5.5 4.1
-
 5-formylfurfural mutant enzyme F412V/W561A, pH and temperature not specified in the publication Pseudomonas putida
1.1.5.5 5
-
 ethanol wild-type enzyme, pH and temperature not specified in the publication Pseudomonas putida
1.1.5.5 5.1
-
 ethanol mutant enzyme F412V/W561A, pH and temperature not specified in the publication Pseudomonas putida
1.1.5.5 5.1
-
 5-(hydroxymethyl)furfural mutant enzyme F412V/W561A, pH and temperature not specified in the publication Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.5.5 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 [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.5.5 0.06
-
 5-(hydroxymethyl)furoic acid mutant enzyme F412V/W561A, pH and temperature not specified in the publication Pseudomonas putida
1.1.5.5 0.38
-
 5-(hydroxymethyl)furfural mutant enzyme F412V/W561A, pH and temperature not specified in the publication Pseudomonas putida
1.1.5.5 0.6
-
 ethanol mutant enzyme F412V/W561A, pH and temperature not specified in the publication Pseudomonas putida
1.1.5.5 1.81
-
 5-formylfurfural mutant enzyme F412V/W561A, pH and temperature not specified in the publication Pseudomonas putida
1.1.5.5 312
-
 ethanol wild-type enzyme, pH and temperature not specified in the publication Pseudomonas putida