Characterization of a Cyanobacterial Haloperoxidase and Evaluation of its Biocatalytic Halogenation Potential | Zendy

Frank Annika | Zendy; Seel Catharina Julia | Zendy; Groll Michael | Zendy; Gulder Tanja | Zendy

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Characterization of a Cyanobacterial Haloperoxidase and Evaluation of its Biocatalytic Halogenation Potential

Author(s) -

Frank Annika,

Seel Catharina Julia,

Groll Michael,

Gulder Tanja

Publication year - 2016

Publication title -

chembiochem

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.05

H-Index - 126

eISSN - 1439-7633

pISSN - 1439-4227

DOI - 10.1002/cbic.201600417

Subject(s) - halogenation , chemistry , biocatalysis , reactivity (psychology) , enzyme , yield (engineering) , combinatorial chemistry , organic chemistry , materials science , catalysis , reaction mechanism , medicine , alternative medicine , pathology , metallurgy

Vanadium‐dependent haloperoxidases (VHPOs) are a class of halogenating enzymes found in fungi, lichen, algae, and bacteria. We report the cloning, purification, and characterization of a functional VHPO from the cyanobacterium Acaryochloris marina ( Am VHPO), including its structure determination by X‐ray crystallography. Compared to other VHPOs, the Am VHPO features a unique set of disulfide bonds that stabilize the dodecameric assembly of the protein. Easy access by high‐yield recombinant expression, as well as resistance towards organic solvents and temperature, together with a distinct halogenation reactivity, make this enzyme a promising starting point for the development of biocatalytic transformations.

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