Presence of a vanadium-dependent haloperoxidase in Botrytis cinerea.
The presence of a haloperoxidase in the mycelium of Botrytis cinerea, extractable with buffer, is demonstrated. A low level of extracellular enzyme activity was also detected. The haloperoxidase from the fungus is a vanadium-dependent glycoprotein, with a pH optimum of about 5.5. Native gel electrophoresis indicates that it is a high molecular mass protein. It appears to react with antibodies against haloperoxidase from Caldariomyces fumago. Enzyme activity is increased 3.5-fold and 15-fold by culture of the fungus in the presence of NaCl or vanadium, respectively. Activity is partly reduced by removal of vanadium and activity can be restored by the addition of vanadium to the enzyme. The possible function of this haloperoxidase is discussed.
Bar-Nun
Nurit
N
Department of Botany, The Hebrew University of Jerusalem, 91904, Jerusalem, Israel.
Shcolnick
Sigal
S
Mayer
Alfred M
AM
D020171:Botrytis / Q000201:enzymology* / Q000302:isolation & purification; D002711:Chloride Peroxidase / Q000032:analysis / Q000378:metabolism*; D003470:Culture Media; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D015151:Immunoblotting / Q000379:methods; D013194:Staining and Labeling; D014639:Vanadium / Q000737:chemistry / Q000494:pharmacology*
D003470:Culture Media; D014639:Vanadium; D002711:Chloride Peroxidase