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Literature summary for 1.1.2.B3 extracted from

  • Arias, S.; Olivera, E.R.; Arcos, M.; Naharro, G.; Luengo, J.M.
    Genetic analyses and molecular characterization of the pathways involved in the conversion of 2-phenylethylamine and 2-phenylethanol into phenylacetic acid in Pseudomonas putida U (2008), Environ. Microbiol., 10, 413-432.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene pedE, DNA and amino acid sequence determination and analysis Pseudomonas putida
gene pedH, DNA and amino acid sequence determination and analysis Pseudomonas putida

Protein Variants

Protein Variants Comment Organism
additional information analysis of Tn5 transposon insertion mutants, genetic organization, overview Pseudomonas putida

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm PedH Pseudomonas putida
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
64870
-
x * 64870, PedH, sequence calculation Pseudomonas putida

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
phenylethanol + ferricytochrome c Pseudomonas putida PedH catalyzes a step in the aerobic transformation of 2-phenylethylamine and 2-phenylethanol. PedH does not belong to the class of PQQ-dependent alcohol dehydrogenases containing a c-type cytochrome heme domain, but to others that transfer electrons to a separate soluble c-type cytochrome phenylacetaldehyde + ferrocytochrome c
-
?

Organism

Organism UniProt Comment Textmining
Pseudomonas putida B1N7J0 PedE; gene pedE
-
Pseudomonas putida B1N7J5 PedH; gene pedH
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phenylethanol + ferricytochrome c PedH catalyzes a step in the aerobic transformation of 2-phenylethylamine and 2-phenylethanol. PedH does not belong to the class of PQQ-dependent alcohol dehydrogenases containing a c-type cytochrome heme domain, but to others that transfer electrons to a separate soluble c-type cytochrome Pseudomonas putida phenylacetaldehyde + ferrocytochrome c
-
?

Subunits

Subunits Comment Organism
? x * 64870, PedH, sequence calculation Pseudomonas putida
More PedH contains a well-conserved PQQ-DH domain, structural analysis Pseudomonas putida

Synonyms

Synonyms Comment Organism
More PedE does not belong to the class of PQQ-dependent alcohol dehydrogenases containing a c-type cytochrome heme domain, but to others that transfer electrons to a separate soluble c-type cytochrome Pseudomonas putida
PedE
-
Pseudomonas putida
PedH
-
Pseudomonas putida
PQQ-alcohol dehydrogenase
-
Pseudomonas putida
PQQ-linked alcohol dehydrogenase
-
Pseudomonas putida

Cofactor

Cofactor Comment Organism Structure
additional information no heme cofactor Pseudomonas putida
pyrroloquinoline quinone PQQ, dependent on, prosthetic group, the consensus sequences involved in the PQQ binding are GAGNPG in PedE, enzymes involved in PQQ biosynthesis are encoded by the pqq gene, e.g. pqqABCDEF, of the pqq cluster Pseudomonas putida
pyrroloquinoline quinone PQQ, dependent on, prosthetic group, the consensus sequences involved in the PQQ binding are GLGVQG and GSGVLG in PedH, enzymes involved in PQQ biosynthesis are encoded by the pqq gene, e.g. pqqABCDEF, of the pqq cluster Pseudomonas putida