Heterologous Expression of the Vanadium-containing Chloroperoxidase from Curvularia inaequalis in Saccharomyces cerevisiae and Site-directed Mutagenesis of the Active Site Residues His496, Lys353, Arg360, and Arg490-Reference-Cited by-同舟云学术

Heterologous Expression of the Vanadium-containing Chloroperoxidase from Curvularia inaequalis in Saccharomyces cerevisiae and Site-directed Mutagenesis of the Active Site Residues His496, Lys353, Arg360, and Arg490

Published:1999-08 Issue:34 Volume:274 Page:23820-23827
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Hemrika Wieger,Renirie Rokus,Macedo-Ribeiro Sandra,Messerschmidt Albrecht,Wever Ron

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference45 articles.

1. The reaction mechanism of the novel vanadium-bromoperoxidase. A steady-state kinetic analysis.

2. Vanadium K-edge x-ray absorption spectroscopy of bromoperoxidase from Ascophyllum nodosum

3. Vanadium chloroperoxidases occur widely in nature

4. The bromoperoxidase from the lichen Xanthoria parietina is a novel vanadium enzyme

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