Journal
CHEMBIOCHEM
Volume 17, Issue 21, Pages 2028-2032Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201600417
Keywords
enzyme catalysis; halogenation; peroxidases; protein structures; vanadium
Funding
- Emmy-Noether program of the German Research Foundation (DFG) [GU 1134/3-1]
- Deutsche Bundesstiftung Umwelt [20015/400]
- [SFB 749]
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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 (AmVHPO), including its structure determination by X-ray crystallography. Compared to other VHPOs, the AmVHPO 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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