Structural and functional comparisons between vanadium haloperoxidase and acid phosphatase enzymes.
The crystallographic structures of both the vanadium chloroperoxidase and bromoperoxidase enzymes have been determined with either vanadium or phosphate bound at their active site. The amino acids that are involved in phosphate binding in the acid phosphatase enzymes and those that are coordinated to vanadium in the haloperoxidases appear to be conserved between the two classes of enzyme. The detailed active site architecture for enzymes that recognize and use either vanadium or phosphate will be discussed in relation to their proposed enzymatic mechanism.
Littlechild
Jennifer
J
Schools of Chemistry and Biological Sciences, University of Exeter, Stocker Road, UK. j.a.littlechild@exeter.ac.uk
Garcia-Rodriguez
Esther
E
Dalby
Andrew
A
Isupov
Misha
M
D000135:Acid Phosphatase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D020134:Catalytic Domain; D002711:Chloride Peroxidase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010544:Peroxidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D010710:Phosphates / Q000737:chemistry; D011487:Protein Conformation; D000461:Rhodophyta / Q000201:enzymology / Q000235:genetics; D017386:Sequence Homology, Amino Acid; D014639:Vanadium / Q000737:chemistry
D010710:Phosphates; D014639:Vanadium; D010544:Peroxidases; C026195:bromide peroxidase; C418625:vanadium chloroperoxidase; D002711:Chloride Peroxidase; D000135:Acid Phosphatase