Reactivation of metal-requiring apoenzymes by phytochelatin-metal complexes.
The enzymatically inactive, metal-requiring apoforms of diamino oxidase and of carbonic anhydrase were reactivated by copper-and zinc-phytochelatin complexes, respectively. The level and the rate of reactivation effected by metal complexes consisting of poly(gamma-glutamylcysteinyl)glycine as well as by the respective free metal ion were compared. An efficient transfer of zinc and copper from phytochelatin-complexes to apoenzymes was observed in vitro.
Thumann
J
J
Lehrstuhl für Pharmazeutische Biologie, Universität München, Germany.
Grill
E
E
Winnacker
E L
EL
Zenk
M H
MH
D006631:Amine Oxidase (Copper-Containing) / Q000378:metabolism*; D001051:Apoenzymes / Q000378:metabolism; D002256:Carbonic Anhydrases / Q000378:metabolism*; D003300:Copper / Q000494:pharmacology*; D004789:Enzyme Activation; D007887:Fabaceae; D007700:Kinetics; D008667:Metalloproteins / Q000494:pharmacology*; D010455:Peptides / Q000494:pharmacology*; D010946:Plants, Medicinal; D015032:Zinc / Q000494:pharmacology*
D001051:Apoenzymes; D008667:Metalloproteins; D010455:Peptides; C016298:chelatin; C053690:poly(gamma-glutamylcysteinyl)glycine; D003300:Copper; D006631:Amine Oxidase (Copper-Containing); D002256:Carbonic Anhydrases; D015032:Zinc