ECB-ART-41786
Acta Biochim Biophys Sin (Shanghai)
2010 Nov 01;4211:779-86. doi: 10.1093/abbs/gmq092.
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Zinc induces unfolding and aggregation of dimeric arginine kinase by trapping reversible unfolding intermediate.
Abstract
Arginine kinase plays an important role in the cellular energy metabolism of invertebrates. Dimeric arginine kinase (dAK) is unique in some marine invertebrates. The effects of Zn²(+) on the unfolding and aggregation of dAK from the sea cucumber Stichopus japonicus were investigated. Our results indicated that Zn²(+) caused dAK inactivation accompanied by conformational unfolding, the exposure of hydrophobic surface, and aggregation. Kinetic studies showed the inactivation and unfolding of dAK followed biphasic kinetic courses. Zn²(+) can affect unfolding and refolding of dAK by trapping the reversible intermediate. Our study provides important information regarding the effect of Zn²(+) on metabolic enzymes in marine invertebrates.
PubMed ID: 20929927
Article link: Acta Biochim Biophys Sin (Shanghai)
Genes referenced: LOC100887844 LOC105440390