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 | Comment | Organism |
---|---|---|
additional information | analysis of Tn5 transposon insertion mutants, genetic organization, overview | Pseudomonas putida |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
periplasm | PedH | Pseudomonas putida | - |
- |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
64870 | - |
x * 64870, PedH, sequence calculation | Pseudomonas putida |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas putida | B1N7J0 | PedE; gene pedE | - |
Pseudomonas putida | B1N7J5 | PedH; gene pedH | - |
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 | Comment | Organism |
---|---|---|
? | x * 64870, PedH, sequence calculation | Pseudomonas putida |
More | PedH contains a well-conserved PQQ-DH domain, structural analysis | Pseudomonas putida |
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 | 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 |