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Literature summary 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)

EC Number Cloned (Comment) Organism
1.1.2.B3 gene pedE, DNA and amino acid sequence determination and analysis Pseudomonas putida
1.1.2.B3 gene pedH, DNA and amino acid sequence determination and analysis Pseudomonas putida
1.2.1.39 Expression in Escherichia coli, production of knock out-mutants is carried out by mutagenesis. Pseudomonas putida
1.4.9.1 Expression in Escherichia coli, the production of knock out-mutants unable to catabolize 2-phenylethylamine is carried out by mutagenesis. Pseudomonas putida

Protein Variants

EC Number Protein Variants Comment Organism
1.1.2.B3 additional information analysis of Tn5 transposon insertion mutants, genetic organization, overview Pseudomonas putida

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.2.B3 periplasm PedH Pseudomonas putida
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.4.9.1 Fe enzyme contains two heme groups Pseudomonas putida

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.2.B3 64870
-
 x * 64870, PedH, sequence calculation Pseudomonas putida
1.2.1.39 53290
-
-
 Pseudomonas putida
1.2.1.39 53290
-
 calculated Pseudomonas putida
1.4.9.1 8579
-
 calculated gamma-subunit Pseudomonas putida
1.4.9.1 39360
-
 calculated for beta-subunit, containing a 26 aa sequence which seems to correspond to a signal peptide that might be also involved in the correct translocation from the bacterial cytoplasm to the periplasmic space. Pseudomonas putida
1.4.9.1 54230
-
 calculated for alpha-subunit, existence in this protein of two consensus sequences (CXXCH) identifying as binding pockets for the two haem groups Pseudomonas putida

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.2.B3 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
-
 ?
1.2.1.39 phenylacetaldehyde + NAD+ + H2O Pseudomonas putida
-
 phenylacetate + NADH + H+
-
 ?
1.2.1.39 phenylacetaldehyde + NAD+ + H2O Pseudomonas putida
-
 phenylacetic acid + NADH + H+
-
 ?
1.4.9.1 2-phenylethylamine + 2 H2O + 2 acceptor Pseudomonas putida primary amine 2-phenylacetic acid + NH3 + 2 reduced acceptor
-
 ?
1.4.9.1 additional information Pseudomonas putida an essential enzyme for the aerobic degradation of many primary amines even though they have quite different chemical structures (aromatic or aliphatic) ?
-
 ?
1.4.9.1 additional information Pseudomonas putida when different QHNDH mutants (peaA, peaC and peaD) are transformed with a genetic construction containing the peaABCD cluster, all the recombinant strains efficiently catabolized 2-phenylethylamine as well as other primary amines like propyl-, butyl- and pentylamine. ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.2.B3 Pseudomonas putida B1N7J0 PedE; gene pedE
-
1.1.2.B3 Pseudomonas putida B1N7J5 PedH; gene pedH
-
1.2.1.39 Pseudomonas putida
-
-
-
1.2.1.39 Pseudomonas putida B1N7H3 U strain, although enzymatic activity decreases in knock-out mutants good phenylacetaldehyde dehydrogenase acivity is present in the bacterium, PeaF and PeaG are suggested to replace PeaE
-
1.4.9.1 Pseudomonas putida
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.2.1.39 cell culture
-
 Pseudomonas putida
-
1.4.9.1 cell culture
-
 Pseudomonas putida
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.2.1.39 additional information
-
 Analysis of phenylacetaldehyde dehydrogenase activity in cell-free extracts reveals that although enzymatic activity decreases in the peaE knocked-out mutant (20% with respect to the control), good phenylacetaldehyde dehydrogenase activity is present. Another aldehyde dehydrogenase(s) exist(s) that could replace the role played by PeaE Pseudomonas putida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.2.B3 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
-
 ?
1.2.1.39 phenylacetaldehyde + NAD+ + H2O
-
 Pseudomonas putida phenylacetate + NADH + H+
-
 ?
1.2.1.39 phenylacetaldehyde + NAD+ + H2O
-
 Pseudomonas putida phenylacetic acid + NADH + H+
-
 ?
1.4.9.1 2-phenylethylamine + 2 H2O + 2 acceptor primary amine Pseudomonas putida 2-phenylacetic acid + NH3 + 2 reduced acceptor
-
 ?
1.4.9.1 additional information an essential enzyme for the aerobic degradation of many primary amines even though they have quite different chemical structures (aromatic or aliphatic) Pseudomonas putida ?
-
 ?
1.4.9.1 additional information when different QHNDH mutants (peaA, peaC and peaD) are transformed with a genetic construction containing the peaABCD cluster, all the recombinant strains efficiently catabolized 2-phenylethylamine as well as other primary amines like propyl-, butyl- and pentylamine. Pseudomonas putida ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.2.B3 ? x * 64870, PedH, sequence calculation Pseudomonas putida
1.1.2.B3 More PedH contains a well-conserved PQQ-DH domain, structural analysis Pseudomonas putida
1.4.9.1 heterotrimer determinated by in silico-experiments, beta-subunit with 349 aa, gamma-subunit with 79 aa and an alpha-subunit with 494 aa Pseudomonas putida
1.4.9.1 More protein PeaB, although not interacting with the active QHNDH along the catalytic reaction, is needed for the correct functionality of this enzyme and for the post-translational modification of the gamma-subunit before its translocation to the periplasmic space. Pseudomonas putida

Synonyms

EC Number Synonyms Comment Organism
1.1.2.B3 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
1.1.2.B3 PedE
-
 Pseudomonas putida
1.1.2.B3 PedH
-
 Pseudomonas putida
1.1.2.B3 PQQ-alcohol dehydrogenase
-
 Pseudomonas putida
1.1.2.B3 PQQ-linked alcohol dehydrogenase
-
 Pseudomonas putida
1.1.5.5 PedE
-
-
1.1.5.5 PedH
-
-
1.1.5.5 PQQ-linked alcohol dehydrogenase
-
-
1.2.1.39 PeaE
-
 Pseudomonas putida
1.2.1.39 PeaE protein
-
 Pseudomonas putida
1.2.1.39 phenylacetaldehyde dehydrogenase
-
 Pseudomonas putida
1.4.9.1 amine dehydrogenase
-
 Pseudomonas putida
1.4.9.1 QH-AmDH
-
 Pseudomonas putida
1.4.9.1 QHNDH
-
 Pseudomonas putida
1.4.9.1 quinohaemoprotein amine dehydrogenase
-
 Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.2.B3 additional information no heme cofactor Pseudomonas putida
1.1.2.B3 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
1.1.2.B3 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
1.2.1.39 NAD+
-
 Pseudomonas putida
1.4.9.1 cysteine tryptophylquinone This enzyme contains an unusual redox cofactor (CTQ) and two hemes acting as redox active groups Pseudomonas putida