i.e. trans-2'-carboxybenzalpyruvate. The structure of the ring cleavage product is determined upon separation by high-performance liquid chromatography at pH 2.5 by using nuclear magnetic resonance and mass spectroscopic techniques
i.e. trans-2'-carboxybenzalpyruvate. The structure of the ring cleavage product is determined upon separation by high-performance liquid chromatography at pH 2.5 by using nuclear magnetic resonance and mass spectroscopic techniques
gentisate 1,2-dioxygenase with an extraordinary substrate range. Relative activities with salicylate, 5-aminosalicylate, 1-hydroxy-2-naphthoate, and gentisate with both preparations are about 1:10:40:120
gentisate 1,2-dioxygenase with an extraordinary substrate range. Relative activities with salicylate, 5-aminosalicylate, 1-hydroxy-2-naphthoate, and gentisate with both preparations are about 1:10:40:120
no inhibition when the concentration of the substrate 1-hydroxy-2-naphthoate is 0.01 mM and that of the tested compounds is 0.1 or 1 mM: gentisate, 3-hydroxyanthranilate, 2-hydroxy-1-naphthoate, salicylate, m-hydroxybenzoate, p-hydroxybenzoate, and protocatechuate
strain Sphe3 grows on 2-carboxybenzaldehyde, protocatechuate, and phthalate as sole carbon sources, all intermediates of phenanthrene degradation via the phthalate pathway, whereas no growth is observed on salicylic acid
strain Sphe3 grows on 2-carboxybenzaldehyde, protocatechuate, and phthalate as sole carbon sources, all intermediates of phenanthrene degradation via the phthalate pathway, whereas no growth is observed on salicylic acid
strain Sphe3 grows on 2-carboxybenzaldehyde, protocatechuate, and phthalate as sole carbon sources, all intermediates of phenanthrene degradation via the phthalate pathway, whereas no growth is observed on salicylic acid
strain Sphe3 grows on 2-carboxybenzaldehyde, protocatechuate, and phthalate as sole carbon sources, all intermediates of phenanthrene degradation via the phthalate pathway, whereas no growth is observed on salicylic acid
occurrence of two diox1 and diox2 homologues in the Sphe3 genome implies that a replicative transposition event has contributed to the evolution of 1-H2NA dioxygenase in Arthrobacter phenanthrenivorans
occurrence of two diox1 and diox2 homologues in the Sphe3 genome implies that a replicative transposition event has contributed to the evolution of 1-H2NA dioxygenase in Arthrobacter phenanthrenivorans
salicylate 1,2-dioxygenase shares with 1-hydroxy-2-naphthoate dioxygenase its unique ability to oxidatively cleave monohydroxylated aromatic compounds. Nevertheless salicylate 1,2-dioxygenase is more versatile with respect to 1-hydroxy-2-naphthoate dioxygenase and other known gentisate dioxygenases because it cleaves not only gentisate and1-hydroxy-2-naphthoate but also salicylate and substituted salicylates, cf. EC 1.13.11.4
salicylate 1,2-dioxygenase shares with 1-hydroxy-2-naphthoate dioxygenase its unique ability to oxidatively cleave monohydroxylated aromatic compounds. Nevertheless salicylate 1,2-dioxygenase is more versatile with respect to 1-hydroxy-2-naphthoate dioxygenase and other known gentisate dioxygenases because it cleaves not only gentisate and1-hydroxy-2-naphthoate but also salicylate and substituted salicylates, cf. EC 1.13.11.4
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant A85H and W104Y variants and mutant W104Y with gentiate, sitting drop vapor diffusion method, 4°C, mixing of 0.001 ml of protein solution with 0.0008 ml of crystallization solution containing 8% PEG10000 and 0.1 M Tris-HCl pH 8.0, with 0.0002 ml of a 0.1 M calcium chloride solution, crystals quality is also improved using seeding techniques, X-ray diffraction structure determination and analysis at 2.5-2.7 A resolution
site-directed mutagenesis, the salicylate 1,2-dioxygenase variant shows higher catalytic efficiencies toward 1-hydroxy-2-naphthoate than the wild-type enzyme and no more activity with gentisate. substitution of Ala85 with a histidine residue caused significant changes in the orientation of the loop containing this residue which is involved in the active site closing upon substrate binding. In SDO A85H this specific loop shifts away from the active site and thus opens the cavity favoring the binding of bulkier substrates. Since this loop also interacts with the N-terminal residues of the vicinal subunit, the structure and packing of the holoenzyme might be also affected.
site-directed mutagenesis, the salicylate 1,2-dioxygenase variant shows higher catalytic efficiencies toward 1-hydroxy-2-naphthoate compared to gentisate than the wild-type enzyme
site-directed mutagenesis, the salicylate 1,2-dioxygenase variant shows increased catalytic efficiencies toward 1-hydroxy-2-naphthoate compared to gentisate and to the wild-type enzyme. W104Y SDO mutant exhibits reduced reaction rates for all substrates
site-directed mutagenesis, the salicylate 1,2-dioxygenase variant shows higher catalytic efficiencies toward 1-hydroxy-2-naphthoate than the wild-type enzyme and no more activity with gentisate. substitution of Ala85 with a histidine residue caused significant changes in the orientation of the loop containing this residue which is involved in the active site closing upon substrate binding. In SDO A85H this specific loop shifts away from the active site and thus opens the cavity favoring the binding of bulkier substrates. Since this loop also interacts with the N-terminal residues of the vicinal subunit, the structure and packing of the holoenzyme might be also affected.
site-directed mutagenesis, the salicylate 1,2-dioxygenase variant shows higher catalytic efficiencies toward 1-hydroxy-2-naphthoate compared to gentisate than the wild-type enzyme
site-directed mutagenesis, the salicylate 1,2-dioxygenase variant shows increased catalytic efficiencies toward 1-hydroxy-2-naphthoate compared to gentisate and to the wild-type enzyme. W104Y SDO mutant exhibits reduced reaction rates for all substrates
generation of a 1-hydroxy-2-naphthoate 1,2-dioxygenase by single point mutation M46V of salicylate 1,2-dioxygenase, rational design of mutants, structure comparisons, overview
generation of a 1-hydroxy-2-naphthoate 1,2-dioxygenase by single point mutation M46V of salicylate 1,2-dioxygenase, rational design of mutants, structure comparisons, overview
gene diox1, gene diox1 is found on an indigenous Sphe3 plasmid, DNA and amino acid sequence determination and analysis, genetic organization, sequence comparisons and phylogenetic tree. The relative RNA transcription level of the chromosomal (diox2) gene is significantly higher than that of its plasmid (diox1) homol, overexpression in Escherichia coli
gene diox2, diox2 is located on the chromosome, DNA and amino acid sequence determination and analysis, genetic organization, sequence comparisons and phylogenetic tree. The relative RNA transcription level of the chromosomal (diox2) gene is significantly higher than that of its plasmid (diox1) homol, overexpression in Escherichia coli
Biochemical and genetic characterization of 2-carboxybenzaldehyde dehydrogenase, an enzyme involved in phenanthrene degradation by Nocardioides sp. strain KP7
Structure of the ring cleavage product of 1-hydroxy-2-naphthoate, an intermediate of the phenanthrene-degradative pathway of Nocardioides sp. strain KP7
Ferraroni, M.; Steimer, L.; Matera, I.; Buerger, S.; Scozzafava, A.; Stolz, A.; Briganti, F.
The generation of a 1-hydroxy-2-naphthoate 1,2-dioxygenase by single point mutations of salicylate 1,2-dioxygenase - rational design of mutants and the crystal structures of the A85H and W104Y variants