Catalytic and Structural Features of Flavoprotein Hydroxylases and Epoxidases

Montersino, S.; Tischler, Dirk; Gassner, George; Berkel, Willem J.H. van

doi:10.1002/adsc.201100384

Cited by 90 publications

(95 citation statements)

References 120 publications

(351 reference statements)

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“…These parahydroxylation enzymes are involved in the degradation pathways of phenolic compounds by bacteria (1,11) or the biosynthetic pathways of antibiotics such as angucyclines and rhodomycin (12,13). 3HB6H from Rhodococcus jostii RHA1 catalyzes the para-hydroxylation of 3-hydroxybenzoate to yield 2,5-dihydroxybenzoate (Fig.…”

Section: °C) This Intermediate Is Subsequently Protonated To Form Amentioning

confidence: 99%

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The Reaction Kinetics of 3-Hydroxybenzoate 6-Hydroxylase from Rhodococcus jostii RHA1 Provide an Understanding of the para-Hydroxylation Enzyme Catalytic Cycle

Sucharitakul

Tongsook

Pakotiprapha

et al. 2013

Journal of Biological Chemistry

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Background: 3-Hydroxybenzoate 6-hydroxylase (3HB6H) is a flavoprotein hydroxylase catalyzing the para-hydroxylation of 3-hydroxybenzoate. Results: The oxidative half-reaction was studied using transient kinetics. The enzyme reaction mechanism was elucidated. Conclusion:The product release and the hydroxylation limit the turnovers and the enzyme shows characteristics different from the ortho-hydroxylation enzymes. Significance: This is the first report on the oxygenation mechanism of a para-hydroxylating flavoenzyme.

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Section: °C) This Intermediate Is Subsequently Protonated To Form Amentioning

confidence: 99%

“…Therefore, the data in this report are useful in identifying that the hydroxylation and product release control the overall catalysis of 3HB6H. Although several flavoenzymes catalyzing para-hydroxylation of aromatic compounds have been reported (11), no detailed kinetic and mechanistic investigations of these enzymes have been carried out.…”

mentioning

confidence: 99%

The Reaction Kinetics of 3-Hydroxybenzoate 6-Hydroxylase from Rhodococcus jostii RHA1 Provide an Understanding of the para-Hydroxylation Enzyme Catalytic Cycle

Sucharitakul

Tongsook

Pakotiprapha

et al. 2013

Journal of Biological Chemistry

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“…This system differs from the typical two-component styrene monooxygenases (StyA/StyB) of pseudomonads by gene fusion as well as by the kinetics and efficiency of styrene epoxidation (22,38,40). Moreover, styA1 and styA2B were not found to be part of a styrene-catabolic operon (styABCD), which raised questions about the existence of a complete styrene-catabolic pathway in strain 1CP.…”

mentioning

confidence: 91%

Styrene Oxide Isomerase of Rhodococcus opacus 1CP, a Highly Stable and Considerably Active Enzyme

Oelschlägel

Gröning

Tischler

et al. 2012

Appl Environ Microbiol

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ABSTRACTStyrene oxide isomerase (SOI) is involved in peripheral styrene catabolism of bacteria and converts styrene oxide to phenylacetaldehyde. Here, we report on the identification, enrichment, and biochemical characterization of a novel representative from the actinobacteriumRhodococcus opacus1CP. The enzyme, which is strongly induced during growth on styrene, was shown to be membrane integrated, and a convenient procedure was developed to highly enrich the protein in active form from the wild-type host. A specific activity of about 370 U mg−1represents the highest activity reported for this enzyme class so far. This, in combination with a wide pH and temperature tolerance, the independence from cofactors, and the ability to convert a spectrum of substituted styrene oxides, makes a biocatalytic application imaginable. First, semipreparative conversions were performed from which up to 760 μmol of the pure phenylacetaldehyde could be obtained from 130 U of enriched SOI. Product concentrations of up to 76 mM were achieved. However, due to the high chemical reactivity of the aldehyde function, SOI was shown to be the subject of an irreversible product inhibition. A half-life of 15 min was determined at a phenylacetaldehyde concentration of about 55 mM, indicating substantial limitations of applicability and the need to modify the process.

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“…In our work we have focused on enzymes from the styrene metabolic pathway of P. putida (S12), an unusually solvent tolerant strain. At the entry point of the styrene pathway, the NADH and FAD–dependent two-component styrene monooxygenase (SMO) transfers an atom from molecular oxygen to the vinyl side chain of styrene to synthesize styrene oxide [7]. This is followed by the transformation of styrene oxide to phenylacetaldehyde (PAL) by the membrane protein, styrene oxide isomerase (SOI) and the NAD + -dependent oxidation of PAL to phenylacetic acid (PAA) by phenylacetaldehyde dehydrogenase (PADH) [8].…”

Section: Introductionmentioning

confidence: 99%

Structure and biochemistry of phenylacetaldehyde dehydrogenase from the Pseudomonas putida S12 styrene catabolic pathway

Crabo

Singh

Nguyen

et al. 2017

Archives of Biochemistry and Biophysics

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Phenylacetaldehyde dehydrogenase catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid in the styrene catabolic and detoxification pathway of Pseudomonas putida (S12). Here we report the structure and mechanistic properties of the N-termininally histidine-tagged enzyme, NPADH. The 2.83Å X-ray crystal structure is similar in fold to sheep liver cytosolic aldehyde dehydrogenase (ALDH1), but has unique set of intersubunit interactions and active site tunnel for substrate entrance. In solution, NPADH occurs as 227 kDa homotetramer. It follows a sequential reaction mechanism in which NAD+ serves as both the leading substrate and homotropic allosteric activator. In the absence of styrene monooxygenase reductase, which regenerates NAD+ from NADH in the first step of styrene catabolism, NPADH is inhibited by a ternary complex involving NADH, product, and phenylacetaldehyde, substrate. Each oligomerization domain of NPADH contains a six-residue insertion that extends this loop over the substrate entrance tunnel of a neighboring subunit, thereby obstructing the active site of the adjacent subunit. This feature could be an important factor in the homotropic activation and product inhibition mechanisms. Compared to ALDH1, the substrate channel of NPADH is narrower and lined with more aromatic residues, suggesting a means for enhancing substrate specificity.

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Catalytic and Structural Features of Flavoprotein Hydroxylases and Epoxidases

Cited by 90 publications

References 120 publications

The Reaction Kinetics of 3-Hydroxybenzoate 6-Hydroxylase from Rhodococcus jostii RHA1 Provide an Understanding of the para-Hydroxylation Enzyme Catalytic Cycle

The Reaction Kinetics of 3-Hydroxybenzoate 6-Hydroxylase from Rhodococcus jostii RHA1 Provide an Understanding of the para-Hydroxylation Enzyme Catalytic Cycle

Styrene Oxide Isomerase of Rhodococcus opacus 1CP, a Highly Stable and Considerably Active Enzyme

Structure and biochemistry of phenylacetaldehyde dehydrogenase from the Pseudomonas putida S12 styrene catabolic pathway

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