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

被引：49

作者：

Frank, Annika ^{[1
,2
]}

Seel, Catharina Julia ^{[1
,2
]}

Groll, Michael ^{[1
,2
]}

Gulder, Tanja ^{[1
,2
]}

机构：

[1] Tech Univ Munich, Dept Chem, Ctr Integrated Prot Sci, Lichtenbergstr 4, D-85747 Garching, Germany

[2] Tech Univ Munich, CRC, Lichtenbergstr 4, D-85747 Garching, Germany

来源：

CHEMBIOCHEM | 2016年 / 17卷 / 21期

关键词：

enzyme catalysis; halogenation; peroxidases; protein structures; vanadium; FUNGUS CURVULARIA-INAEQUALIS; VANADIUM-DEPENDENT BROMOPEROXIDASE; ALGAE CORALLINA-OFFICINALIS; STATE KINETIC-ANALYSIS; X-RAY-STRUCTURE; ASCOPHYLLUM-NODOSUM; SACCHAROMYCES-CEREVISIAE; RECOMBINANT ENZYME; REACTION-MECHANISM; CHLOROPEROXIDASE;

D O I：

10.1002/cbic.201600417

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：2028 / 2032

页数：5

共 61 条

[1] BASIC LOCAL ALIGNMENT SEARCH TOOL [J].