Indolyl-3-acetaldoxime dehydratase from the phytopathogenic fungus Sclerotinia sclerotiorum: Purification, characterization, and substrate specificity

Pedras, M. Soledade C.; Minić, Zoran; Thongbam, Premila Devi; Bhaskar, V.; Montaut, Sabine

doi:10.1016/j.phytochem.2010.10.002

Cited by 22 publications

(14 citation statements)

References 39 publications

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“…4‐(Indol‐3‐yl)butanal 1 was synthesized according to a known procedure and the 1 H NMR data are identical with the corresponding data in the literature.…”

Section: Methodsmentioning

confidence: 84%

Enatioselective Synthesis of Tetrahydrocarbazoles via Chiral Phosphoric Acid Promoted Domino Friedel–Crafts‐type Reaction of Indole‐3‐butanal with Indoles

Shibata

Chen

et al. 2018

Journal of Heterocyclic Chem

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“…4‐(Indol‐3‐yl)butanal 1 was synthesized according to a known procedure and the 1 H NMR data are identical with the corresponding data in the literature.…”

Section: Methodsmentioning

confidence: 84%

Enatioselective Synthesis of Tetrahydrocarbazoles via Chiral Phosphoric Acid Promoted Domino Friedel–Crafts‐type Reaction of Indole‐3‐butanal with Indoles

Shibata

Chen

et al. 2018

Journal of Heterocyclic Chem

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“…Three members of the Oxd family working as hydrolyases are registered in the Enzyme Structures Database, namely aliphatic aldoxime dehydratase, [65] phenylacetaldoxime dehydratase, [66] and indolyl-3-acetaldoxime dehydratase. [67,68] All Oxd enzymes purified from different microorganisms exhibit a relatively broad substrate scope, accepting both Eand Z-aldoximes with alkyl or aryl substituents. Nitriles are important intermediates in some industrial processes to produce nylon, acrylic fibers, insecticides, and phar-maceuticals.…”

Section: Aldoxime Dehydratasesmentioning

confidence: 99%

“…Scheme 17 Substrate Specificity of Oxd Enzymes [66,68,69,[73][74][75] [66] Bn Z OxdRE b 100 [69] Bn Z OxdFG c 100 [73] Bn Z OxdK d 93 [74] CHMePh E/Z OxdRE b 50 [69] CHMePh E/Z OxdFG c 69 [73] CHMePh E/Z OxdK d 280 [74] (CH 2 ) 2 Ph Z Oxd a 63 [66] (CH 2 ) 2 Ph Z OxdRE b 70 [69] (CH 2 ) 2 Ph Z OxdFG c 104 [73] (CH 2 ) 2 Ph Z OxdK d 452 [74] (CH 2 ) 3 Ph E/Z Oxd a 6.8 [66] (CH 2 ) 3 Ph E/Z OxdRE b 29 [69] (CH 2 ) 3 Ph E/Z OxdFG c 79 [73] 2-pyridyl E/Z Oxd e 2.4 [75] 3-pyridyl E/Z Oxd e 18 (Z)/100 (E) [75] 3-pyridyl E/Z OxdRE b 0.5 (E) [69] N N E Oxd e 5.5 [75] 4-Tol E Oxd e 1.1 [75] 4-Tol E OxdRE b 0.5 [69] 4-ClC 6 H 4 E Oxd a 7.4 [66] 4-ClC 6 H 4 E Oxd e 1 [75] 4-ClC 6 H 4 E OxdRE b 3.4 [69] 4-MeOC 6 H 4 E Oxd a 6.8 [66] 4-MeOC 6 H 4 E Oxd e 0.2 [75] 4-O 2 NC 6 H 4 E Oxd e 0.2 [75] Z Oxd a 4.5 [66] Z OxdRE b 2.7 [69] CHPhOH E/Z OxdRE b 12 [69] CHPhOH E/Z OxdFG c 16 [73] CHPhOH E/Z OxdK d 29 [74] (E)-CH=CHPh E/Z OxdRE b 4.3 [65] [74] 1H-indol-3-yl E/Z Oxd a 18 [66] 1H-indol-3-yl E/Z Oxd e 0.3 [75] 1H-indol-3-yl E/Z OxdRE b 42 …”

Section: Mechanismmentioning

confidence: 99%

3.10 Emerging Enzymes

Glueck,

Hammer,

Hauer

et al. 2015

Biocatalysis in Organic Synthesis 3

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The broad application of enzymes in industry is still impeded by the limited repertoire of available enzymes. New applications of biocatalysts in a sustainable bio-based economy, especially for employment in bioremediation, bioenergy, and bioproducts, appear to be the driving force behind the increased prevalence of novel enzymatic catalysts. Advances in synthetic biology, enzyme engineering, de novo enzyme (re)design, exploitation of enzyme promiscuity, and DNA sequencing technologies show great potential to facilitate the development of more efficient enzymes. Combined efforts would have the following benefits: an increased range of biocatalysts with different catalytic activities would be available and more biocatalysts with improved characteristics suitable for (bio)synthetic chemistry approaches would be discovered. This chapter demonstrates the potential of enzymes that have been investigated recently, but not yet fully exploited, for applications in chemical synthesis: nitrile reductases, sulfatases, phenol-coupling monooxygenases, squalene hopene cyclases, and aldoxime dehydratases. Examples of emerging enzymes and microorganisms that have been studied over the last few years and that have acquired scientific as well as industrial interest are described to illustrate the synthetic potential of these biocatalysts.The screening reactions were run in UV star 96-well plates using recombinant His-tagged enzymes purified via nickel affinity chromatography. The following conditions were applied: nitrile reductase (45 ìM, purity >85%) in buffer [100 mM Tris, 50 mM KCl, 1.15 mM 3.10.

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“…12−14 Three members of the Oxd family are registered in the Enzyme Structure Database, namely aliphatic aldoxime dehydratase, 15 phenylacetaldoxime dehydratase, 3 and indolyl-3-acetaldoxime dehydratase. 16,17 All Oxd enzymes purified from different microorganisms exhibit a relatively broad substrate scope, accepting both E/Z types of aldoximes with alkyl or aryl substituents. 2,3,15,18−22 The crystal structures of wild-type Oxd from Rhodococcus sp.…”

Section: Introductionmentioning

confidence: 99%

Why Is the Oxidation State of Iron Crucial for the Activity of Heme-Dependent Aldoxime Dehydratase? A QM/MM Study

Liao

Thiel

2012

J. Phys. Chem. B

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Aldoxime dehydratase is a heme-containing enzyme that utilizes the ferrous rather than the ferric ion to catalyze the synthesis of nitriles by dehydration of the substrate. We report a theoretical study of this enzyme aimed at elucidating its catalytic mechanism and understanding this oxidation state preference (Fe 2+ versus Fe 3+ ). The uncatalyzed dehydration reaction was modeled by including three and four water molecules to assist in the proton transfer, but the computed barriers were very high at both the DFT (B3LYP) and coupled cluster CCSD(T) levels. The enzymatic dehydration of Z-acetaldoxime was explored through QM/MM calculation using two different QM regions and covering all three possible spin states. The reaction starts by substrate coordination to Fe 2+ via its nitrogen atom to form a six-coordinated singlet reactant complex. The ferrous heme catalyzes the N−O bond cleavage by transferring one electron to the antibond in the singlet state, while His320 functions as a general acid to deliver a proton to the leaving hydroxide, thus facilitating its departure. The key intermediate is identified as an Fe III (CH 3 CHN • ) species (triplet or open-shell singlet), with the closed-shell singlet Fe II (CH 3 CHN + ) being about 6 kcal/mol higher. Subsequently, the same His320 residue abstracts the α-proton, coupled with electron transfer back to the iron center. Both steps are calculated to have feasible barriers (14−15 kcal/mol), in agreement with experimental kinetic studies. For the same mode of substrate coordination, the ferric heme does not catalyze the N−O bond cleavage, because the reaction is endothermic by about 40 kcal/mol, mainly due to the energetic penalty for oxidizing the ferric heme. The alternative binding option, in which the anionic aldoxime coordinates to the ferric ion via its oxyanion, also results in a high barrier (around 30 kcal/mol), mainly because of the large endothermicity associated with the generation of a suitable base (neutral His320) for proton abstraction.

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Indolyl-3-acetaldoxime dehydratase from the phytopathogenic fungus Sclerotinia sclerotiorum: Purification, characterization, and substrate specificity

Cited by 22 publications

References 39 publications

Enatioselective Synthesis of Tetrahydrocarbazoles via Chiral Phosphoric Acid Promoted Domino Friedel–Crafts‐type Reaction of Indole‐3‐butanal with Indoles

Enatioselective Synthesis of Tetrahydrocarbazoles via Chiral Phosphoric Acid Promoted Domino Friedel–Crafts‐type Reaction of Indole‐3‐butanal with Indoles

3.10 Emerging Enzymes

Why Is the Oxidation State of Iron Crucial for the Activity of Heme-Dependent Aldoxime Dehydratase? A QM/MM Study

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