EC Number   |
General Information |
Reference |
|---|
    1.14.13.1 | evolution |
phylogenetic analysis and tree, salicylate hydroxylase homologue FgShy1 is most closely related to NahG from Pseudomonas putida and Shy1 from Ustilago maydis |
-, 764734 |
| 1.14.13.1 | evolution |
phylogenetic analysis and tree, salicylate hydroxylase homologue FgShyC is unique to the North American population 2 (NA2), FgShyC is present only in NA2 strains |
-, 764734 |
| 1.14.13.1 | evolution |
the enzyme reaction links the upper and lower pathways of naphthalene degradation by soil pseudomonads, a bacterial genus encompassing many species that can use naphthalene or salicylate as sole carbon sources. NahG hydroxylates and decarboxylates the substrate at the same aromatic carbon atom (ipso substitution), an exquisite feature that is remarkable from a synthetic perspective. NahG is one of the few examples of a flavin enzyme that catalyzes an ortho hydroxylation relative to the substrate's phenol group, which is usually required for efficient catalysis. Other monooxygenases exhibit different regioselectivities. Enzyme structure comparisons, overview. The aromatic residues F85,W87, F230, F243, and W293 are positioned on the antiparallel beta-sheet opposite from the FAD isoalloxazine ring and likely form a hydrophobic environment facing the salicylate. In addition, a number of nonpolar amino acid residues, including A190, M194, M219, L221, L228, and V241, also compose the substrate-binding pocket, whereas the charged residues D224, H226, R247, H322, E381, and R383 are distinctly grouped near the active site, laterally positioned on the re-side of the isoalloxazine and leading to the solvent-accessible protein surface |
-, 764872 |
| 1.14.13.1 | evolution |
the NahG homologue from tomato (SlSA1H) belongs to the FAD/NAD(P)-binding oxidoreductase family and is capable of catalyzing the oxidative decarboxylation (i.e. 1-hydroxylation) of SA to catechol both in vitro and in planta. Phylogenetic tree, overview |
765597 |
| 1.14.13.1 | malfunction |
a mutant strain with multiple copies of salA exhibits elevated expression of salA and increased terbinafine resistance |
-, 765315 |
| 1.14.13.1 | malfunction |
deletion of shyA, dhbA, and crcA in Aspergillus niger results in reduced growth on salicylic acid, 2,3-dihydroxybenzoic acid, and catechol, respectively, confirming their in vivo roles |
-, 763980 |
| 1.14.13.1 | metabolism |
in the filamentous fungus Aspergillus niger, two salicylic acid metabolic pathways have been suggested. The first pathway converts salicylic acid to catechol by a salicylate hydroxylase (ShyA). In the second pathway, salicylic acid is 3-hydroxylated to 2,3-dihydroxybenzoic acid, followed by decarboxylation to catechol by 2,3-dihydroxybenzoate decarboxylase (DhbA). ShyA, DhbA, and CrcA are involved in the fungal salicylic acid pathway, overview. The recombinant ShyA and CrcA together can efficiently convert salicylic acid into cis,cis-muconic acid through catechol as an intermediate. NRRL3_43 is suggested to be a salicylic acid hydroxylase-like enzyme |
-, 763980 |
| 1.14.13.1 | metabolism |
naphthalene degradation |
-, 698002 |
| 1.14.13.1 | metabolism |
salicylate 1-hydroxylase is not clustered with the meta cleavage pathway |
680483 |
| 1.14.13.1 | metabolism |
salicylate hydroxylase (NahG) is a flavin-dependent monooxygenase that catalyzes the decarboxylative hydroxylation of salicylate into catechol in the naphthalene degradation pathway in Pseudomonas putida strain G7 with stoichiometric consumption of NADH and O2. This reaction links the upper and lower pathways of naphthalene degradation by soil pseudomonads, a bacterial genus encompassing many species that can use naphthalene or salicylate as sole carbon sources |
-, 764872 |
