Structural highlights
Publication Abstract from PubMed
Vanadium-dependent haloperoxidases (VHPOs) are an exquisite 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. The AmVHPO features a unique set of disulfide bonds, which 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.
Characterization of a Cyanobacterial Haloperoxidase and Evaluation of its Biocatalytic Halogenation Potential.,Frank A, Seel CJ, Groll M, Gulder T Chembiochem. 2016 Aug 19. doi: 10.1002/cbic.201600417. PMID:27542168[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Frank A, Seel CJ, Groll M, Gulder T. Characterization of a Cyanobacterial Haloperoxidase and Evaluation of its Biocatalytic Halogenation Potential. Chembiochem. 2016 Aug 19. doi: 10.1002/cbic.201600417. PMID:27542168 doi:http://dx.doi.org/10.1002/cbic.201600417
