Enzymatic Kolbe–Schmitt reaction to form salicylic acid from phenol: Enzymatic characterization and gene identification of a novel enzyme, Trichosporon moniliiforme salicylic acid decarboxylase

Kirimura, Kohtaro; Gunji, Hiroaki; Wakayama, Rumiko; Hattori, Takasumi; Ishii, Yoshitaka

doi:10.1016/j.bbrc.2010.02.154

Cited by 77 publications

(49 citation statements)

References 19 publications

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“…2,6‐Dihydroxybenzoate decarboxylase (2,6‐DHBD_Rs; Rhizobium sp . )54 and salicylic acid decarboxylase (SAD Tm; Trichosporon moniliiforme )55 were also found to be efficient for the carboxylation process. The phenolic acid decarboxylase derived from Lactobacillus plantarum (PAD_Lp)56 and Bacillus amyloliquefaciens (PAD_Ba)57 selectively acted at the β‐carbon atom of styrenes forming ( E )‐cinnamic acids.…”

Section: Introductionmentioning

confidence: 99%

C−H Carboxylation of Aromatic Compounds through CO₂ Fixation

2017

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Carbon dioxide (CO2) represents the most abundant and accessible carbon source on Earth. Thus the ability to transform CO2 into valuable commodity chemicals through the construction of C−C bonds is an invaluable strategy. Carboxylic acids and derivatives, the main products obtained by carboxylation of carbon nucleophiles by reaction of CO2, have wide application in pharmaceuticals and advanced materials. Among the variety of carboxylation methods currently available, the direct carboxylation of C−H bonds with CO2 has attracted much attention owing to advantages from a step‐ and atom‐economical point of view. In particular, the prevalence of (hetero)aromatic carboxylic acids and derivatives among biologically active compounds has led to significant interest in the development of methods for their direct carboxylation from CO2. Herein, the latest achievements in the area of direct C−H carboxylation of (hetero)aromatic compounds with CO2 will be discussed.

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Section: Introductionmentioning

confidence: 99%

C−H Carboxylation of Aromatic Compounds through CO₂ Fixation

2017

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“…The carboxylation of (hetero)aromatic and phenolic compounds is a convenient method to obtain aromatic carboxylic acids used as pharmaceuticals1,2 (e.g., salicylic and m ‐aminosalicylic acid) as well as building blocks for organic synthesis. The traditional chemical (Kolbe–Schmitt) carboxylation process performed on an industrial scale requires high pressure and temperature (∼90 bar, 120–300 °C) and often suffers from incomplete regioselectivities resulting in product mixtures 3.…”

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“…To date, a biocatalytic toolbox for the regioselective ortho ‐,1,2,8 para ‐9 and β‐carboxylation10 of phenols and hydroxystyrenes, respectively, has been established, which employs decarboxylases acting in the (reverse) carboxylation direction using bicarbonate as CO 2 source. In addition, electron‐rich heteroaromatics, such as pyrrole and indole were successfully carboxylated 11.…”

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Regioselective Enzymatic Carboxylation of Bioactive (Poly)phenols

et al. 2017

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In order to extend the applicability of the regioselective enzymatic carboxylation of phenols, the substrate scope of o‐benzoic acid (de)carboxylases has been investigated towards complex molecules with an emphasis on flavouring agents and polyphenols possessing antioxidant properties. o‐Hydroxycarboxylic acid products were obtained with perfect regioselectivity, in moderate to excellent yields. The applicability of this method was proven by the regioselective bio‐carboxylation of resveratrol on a preparative scale with 95% yield.

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“…On the other hand, oxygen-insensitive decarboxylases, such as 2,3-dihydroxybenzoate decarboxylase (14), 5-carboxyvanillate decarboxylase (4), and 4,5-dihydroxyphthalate decarboxylase (8), have been reported to catalyze the decarboxylation reaction only. However, there are a few nonoxidative oxygen-insensitive decarboxylases, viz., ␥-resorcylate decarboxylase (15), vanillate/4-hydroxybenzoate decarboxylase (16), and salicylate decarboxylase (17), that have been documented to catalyze reversible reactions.…”

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Functional Characterization of a Novel Member of the Amidohydrolase 2 Protein Family, 2-Hydroxy-1-Naphthoic Acid Nonoxidative Decarboxylase from Burkholderia sp. Strain BC1

et al. 2016

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The gene encoding a nonoxidative decarboxylase capable of catalyzing the transformation of 2-hydroxy-1-naphthoic acid (2H1NA) to 2-naphthol was identified, recombinantly expressed, and purified to homogeneity. The putative gene sequence of the decarboxylase (hndA) encodes a 316-amino-acid protein (HndA) with a predicted molecular mass of 34 kDa. HndA exhibited high identity with uncharacterized amidohydrolase 2 proteins of various Burkholderia species, whereas it showed a modest 27% identity with ␥-resorcylate decarboxylase, a well-characterized nonoxidative decarboxylase belonging to the amidohydrolase superfamily. Biochemically characterized HndA demonstrated strict substrate specificity toward 2H1NA, whereas inhibition studies with HndA indicated the presence of zinc as the transition metal center, as confirmed by atomic absorption spectroscopy. A three-dimensional structural model of HndA, followed by docking analysis, identified the conserved metal-coordinating and substrate-binding residues, while their importance in catalysis was validated by site-directed mutagenesis. IMPORTANCEMicrobial nonoxidative decarboxylases play a crucial role in the metabolism of a large array of carboxy aromatic chemicals released into the environment from a variety of natural and anthropogenic sources. Among these, hydroxynaphthoic acids are usually encountered as pathway intermediates in the bacterial degradation of polycyclic aromatic hydrocarbons. The present study reveals biochemical and molecular characterization of a 2-hydroxy-1-naphthoic acid nonoxidative decarboxylase involved in an alternative metabolic pathway which can be classified as a member of the small repertoire of nonoxidative decarboxylases belonging to the amidohydrolase 2 family of proteins. The strict substrate specificity and sequence uniqueness make it a novel member of the metallo-dependent hydrolase superfamily. Decarboxylase is one of the most important classes of enzymes involved in a large variety of catabolic and anabolic pathways. The majority of the decarboxylases utilize an organic cofactor or a transition metal coupled with dioxygen to activate their substrates leading to the removal of carbon dioxide (1). However, there is a small group of transition metal-dependent decarboxylases that carry out decarboxylation of various aromatic acids in a nonoxidative manner. These nonoxidative decarboxylases act on various lignin-derived compounds, such as 4-hydroxybenzoic acid (2), (carboxy)vanillic acid (3, 4), protocatechuic acid (5), ferulic acid (6), p-coumaric acid (7), and estrogenic phthalate (8). Likewise, oxygen-independent decarboxylases are also involved in the 2-nitrobenzoic acid degradation pathway (9, 10), the tryptophan catabolic pathway (11), and the thymidine salvage pathway (12).Nonoxidative decarboxylases, in general, can broadly be classified into two major groups depending on their oxygen sensitivity. Oxygen-sensitive decarboxylases, viz., 4-hydroxybenzoate decarboxylase (2), 3,4-dihydroxybenzoate decarboxylase (5), and indol...

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Enzymatic Kolbe–Schmitt reaction to form salicylic acid from phenol: Enzymatic characterization and gene identification of a novel enzyme, Trichosporon moniliiforme salicylic acid decarboxylase

Cited by 77 publications

References 19 publications

C−H Carboxylation of Aromatic Compounds through CO₂ Fixation

C−H Carboxylation of Aromatic Compounds through CO₂ Fixation

Regioselective Enzymatic Carboxylation of Bioactive (Poly)phenols

Functional Characterization of a Novel Member of the Amidohydrolase 2 Protein Family, 2-Hydroxy-1-Naphthoic Acid Nonoxidative Decarboxylase from Burkholderia sp. Strain BC1

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Enzymatic Kolbe–Schmitt reaction to form salicylic acid from phenol: Enzymatic characterization and gene identification of a novel enzyme, Trichosporon moniliiforme salicylic acid decarboxylase

Cited by 77 publications

References 19 publications

C−H Carboxylation of Aromatic Compounds through CO2 Fixation

C−H Carboxylation of Aromatic Compounds through CO2 Fixation

Regioselective Enzymatic Carboxylation of Bioactive (Poly)phenols

Functional Characterization of a Novel Member of the Amidohydrolase 2 Protein Family, 2-Hydroxy-1-Naphthoic Acid Nonoxidative Decarboxylase from Burkholderia sp. Strain BC1

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C−H Carboxylation of Aromatic Compounds through CO₂ Fixation

C−H Carboxylation of Aromatic Compounds through CO₂ Fixation