AI Article Synopsis
- Vanadium-dependent haloperoxidases (VHPOs) are enzymes found in various organisms like fungi and bacteria, and this study focuses on characterizing a specific VHPO from the cyanobacterium Acaryochloris marina (AmVHPO).
- AmVHPO is notable for its unique disulfide bonds that support its dodecameric structure, providing stability compared to other VHPOs.
- Its properties, such as high yield from recombinant expression, resistance to solvents and temperature, and unique halogenation reactivity, suggest it has potential for use in biocatalytic applications.
Article Abstract
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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| http://dx.doi.org/10.1002/cbic.201600417 | DOI Listing |
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