Flavoprotein Oxidases

Ouedraogo, Daniel; Gadda, Giovanni

doi:10.1002/9783527830138.ch9

Cited by 2 publications

(1 citation statement)

References 72 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It is striking, therefore, that loop truncation near the active site of Cgr AAO resulted in a radical switch in regioselectivity to generate a competent C-1 carbohydrate oxidase. Given the abundance of AA5 members with extended loops, it remains to be seen whether similar protein engineering can be used to generate other biocatalysts as alternatives to the widely used flavo-oxidases for applications. , The breadth of substrate preferences now known for wild-type CROs, coupled with the ability to modify specificity, as exemplified here and previously, underscores the versatility and potential of this family of enzymes.…”

Section: Discussionmentioning

confidence: 99%

Active-Site Engineering Switches Carbohydrate Regiospecificity in a Fungal Copper Radical Oxidase

2022

View full text Add to dashboard Cite

Copper radical oxidases (CROs) from Auxiliary Activity Family 5, Subfamily 2 (AA5_2), are organic cofactor-free biocatalysts for the selective oxidation of alcohols to the corresponding aldehydes. AA5_2 CROs comprise canonical galactose-6-oxidases as well as the more recently discovered general alcohol oxidases and aryl alcohol oxidases. Guided by primary and tertiary protein structural analyses, we targeted a distinct extended loop in the active site of a Colletotrichum graminicola aryl alcohol oxidase (CgrAAO) to explore its effect on catalysis in the broader context of AA5_2. Deletion of this loop, which is bracketed by a conserved disulfide bridge, significantly reduced the inherent activity of the enzyme toward extended galacto-oligosaccharides, as anticipated from molecular modeling. Unexpectedly, kinetic and product analysis on a range of monosaccharides and disaccharides revealed that an altered carbohydrate specificity in CgrAAO-Δloop was accompanied by a complete change in regiospecificity from C-6 to C-1 oxidation, thereby generating aldonic acids. C-1 regiospecificity is unprecedented in AA5 enzymes and is classically associated with flavin-dependent carbohydrate oxidases of Auxiliary Activity Family 3. Thus, this work further highlights the catalytic adaptability of the unique mononuclear copper radical active site and provides a basis for the design of improved biocatalysts for diverse potential applications.

show abstract

Section: Discussionmentioning

confidence: 99%

Active-Site Engineering Switches Carbohydrate Regiospecificity in a Fungal Copper Radical Oxidase

2022

View full text Add to dashboard Cite

show abstract

Flavin‐Catalyzed Aerobic Oxidative C−C Bond Formation by Metal/Light‐Free Cross‐Dehydrogenative Coupling

Miyake,

Iida

2023

Adv Synth Catal

View full text Add to dashboard Cite

Biomimetic flavin catalysts enable green and selective aerobic oxidative transformations. However, most previous studies tended to focus on reproducing the enzymatic function of flavin monooxygenase, thereby limiting the applications of flavin catalysts to oxygen‐atom transfer reactions. We herein report a cross‐dehydrogenative coupling (CDC) between the sp3 C−H bond of tetrahydroisoquinolines and the sp3 and sp2 C−H bonds of carbon nucleophiles, such as α‐methylene carbonyl compounds, nitromethane, and indoles, for C−C bond formation promoted by flavin catalysts. Flavin catalysis enables the oxidative C−H activation of tetrahydroisoquinolines and the efficient activation of molecular oxygen (1 atm) under mild and metal/light‐free conditions, thus facilitating a green aerobic CDC that generates benign water as the sole by‐product.

show abstract

Flavoprotein Oxidases

Cited by 2 publications

References 72 publications

Active-Site Engineering Switches Carbohydrate Regiospecificity in a Fungal Copper Radical Oxidase

Active-Site Engineering Switches Carbohydrate Regiospecificity in a Fungal Copper Radical Oxidase

Flavin‐Catalyzed Aerobic Oxidative C−C Bond Formation by Metal/Light‐Free Cross‐Dehydrogenative Coupling

Contact Info

Product

Resources

About