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evolution
phylogenetic analysis and tree, salicylate hydroxylase homologue FgShy1 is most closely related to NahG from Pseudomonas putida and Shy1 from Ustilago maydis
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
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
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
evolution
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phylogenetic analysis and tree, salicylate hydroxylase homologue FgShy1 is most closely related to NahG from Pseudomonas putida and Shy1 from Ustilago maydis
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evolution
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phylogenetic analysis and tree, salicylate hydroxylase homologue FgShyC is unique to the North American population 2 (NA2), FgShyC is present only in NA2 strains
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evolution
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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
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evolution
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phylogenetic analysis and tree, salicylate hydroxylase homologue FgShy1 is most closely related to NahG from Pseudomonas putida and Shy1 from Ustilago maydis
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evolution
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phylogenetic analysis and tree, salicylate hydroxylase homologue FgShy1 is most closely related to NahG from Pseudomonas putida and Shy1 from Ustilago maydis
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evolution
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phylogenetic analysis and tree, salicylate hydroxylase homologue FgShy1 is most closely related to NahG from Pseudomonas putida and Shy1 from Ustilago maydis
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evolution
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phylogenetic analysis and tree, salicylate hydroxylase homologue FgShy1 is most closely related to NahG from Pseudomonas putida and Shy1 from Ustilago maydis
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malfunction
a mutant strain with multiple copies of salA exhibits elevated expression of salA and increased terbinafine resistance
malfunction
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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
malfunction
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a mutant strain with multiple copies of salA exhibits elevated expression of salA and increased terbinafine resistance
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malfunction
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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
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metabolism
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naphthalene degradation
metabolism
salicylate 1-hydroxylase is not clustered with the meta cleavage pathway
metabolism
strain MT1 is capable of degrading 4- and 5-chlorosalicylates via 4-chlorocatechol, 3-chloromuconate, and maleylacetate by the chlorocatechol pathway, overview
metabolism
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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
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
metabolism
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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
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metabolism
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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
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metabolism
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naphthalene degradation
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physiological function
enzyme activity is needed for growth on plates with salicylic acid as a sole carbon source. Enzyme does not contribute significantly to virulence in a seedling infection assay
physiological function
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expression of enzyme gene in Arabidopsis thaliana, with chloroplast targeting sequence. Plants expressing NahG gene in the chloroplasts are unable to accumulate salicylic acid induced after pathogen or UV exposure. The decreased levels in chloroplast-targeted NahG are in the same range as those observed in transgenic plants expressing NahG in the cytosol. Data infer that salicylic acid is initially located in the chloroplasts
physiological function
FgShy1 is not essential for the growth of Fusarium graminearum on agar medium with SA, suggesting additional enzymes or other SA degradation pathways exist
physiological function
in plants, salicylate (SA) is best known as an important phytohormone involved in the activation of defense response against a wide range of biotic and abiotic stresses. Besides its role in immune responses, SA also plays crucial roles in plant growth and developmental processes such as photosynthesis, flowering, and senescence. Because of its chemical reactivity, lipophilicity, and phytotoxicity, most of the SA synthesized in plants is further modified into different derivatives to fine-tune its storage, function, and/or mobility. These modifications include glycosylation, methylation, sulfonation, amino acid conjugation, and hydroxylation. Enzyme SlSA1H may play an important role in the homeostasis of SA in vivo
physiological function
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
physiological function
salicylate hydroxylase (SALH) is a member of oxygen oxidoreductases, which catalyzes the hydroxylation and decarboxylation of salicylate to generate catechol
physiological function
the salA gene, encoding salicylate 1-monooxygenase, is involved in resistance of the dermatophyte Trichophyton rubrum to terbinafine (TRB), one of the most effective antifungal drugs against dermatophytes. Resistance to TRB is mediated by multiple salA copies in Trichophyton rubrum. Salicylate 1-monooxygenase is an enzyme that participates in the naphthalene degradation pathway, converting the intermediate metabolite salicylic acid into catechol
physiological function
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the salA gene, encoding salicylate 1-monooxygenase, is involved in resistance of the dermatophyte Trichophyton rubrum to terbinafine (TRB), one of the most effective antifungal drugs against dermatophytes. Resistance to TRB is mediated by multiple salA copies in Trichophyton rubrum. Salicylate 1-monooxygenase is an enzyme that participates in the naphthalene degradation pathway, converting the intermediate metabolite salicylic acid into catechol
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physiological function
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FgShy1 is not essential for the growth of Fusarium graminearum on agar medium with SA, suggesting additional enzymes or other SA degradation pathways exist
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physiological function
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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
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physiological function
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expression of enzyme gene in Arabidopsis thaliana, with chloroplast targeting sequence. Plants expressing NahG gene in the chloroplasts are unable to accumulate salicylic acid induced after pathogen or UV exposure. The decreased levels in chloroplast-targeted NahG are in the same range as those observed in transgenic plants expressing NahG in the cytosol. Data infer that salicylic acid is initially located in the chloroplasts
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physiological function
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enzyme activity is needed for growth on plates with salicylic acid as a sole carbon source. Enzyme does not contribute significantly to virulence in a seedling infection assay
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physiological function
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FgShy1 is not essential for the growth of Fusarium graminearum on agar medium with SA, suggesting additional enzymes or other SA degradation pathways exist
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physiological function
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FgShy1 is not essential for the growth of Fusarium graminearum on agar medium with SA, suggesting additional enzymes or other SA degradation pathways exist
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physiological function
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FgShy1 is not essential for the growth of Fusarium graminearum on agar medium with SA, suggesting additional enzymes or other SA degradation pathways exist
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physiological function
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salicylate hydroxylase (SALH) is a member of oxygen oxidoreductases, which catalyzes the hydroxylation and decarboxylation of salicylate to generate catechol
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physiological function
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FgShy1 is not essential for the growth of Fusarium graminearum on agar medium with SA, suggesting additional enzymes or other SA degradation pathways exist
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additional information
struccture-function relationship and reaction mechansim analysis, overview. Hammett plots for Km and kcat using substituted salicylates indicate changes in rate-limiting step. Electron-donating groups favor the hydroxylation of salicylate by a peroxyflavin to yield a Wheland-like intermediate, whereas the decarboxylation of this intermediate is faster for electron-withdrawing groups
additional information
structure-function relationship and analysis using combined quantum mechanical/molecular mechanical (QM/MM) calculations, overview
additional information
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struccture-function relationship and reaction mechansim analysis, overview. Hammett plots for Km and kcat using substituted salicylates indicate changes in rate-limiting step. Electron-donating groups favor the hydroxylation of salicylate by a peroxyflavin to yield a Wheland-like intermediate, whereas the decarboxylation of this intermediate is faster for electron-withdrawing groups
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additional information
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structure-function relationship and analysis using combined quantum mechanical/molecular mechanical (QM/MM) calculations, overview
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