Abstract:
:Arginine kinase plays an important role in cellular energy metabolism and is closely related to the environmental stress response in marine invertebrates. We studied the Cu(2+)-mediated inhibition and aggregation of Sepia pharaonis arginine kinase (SPAK) and found that Cu(2+) markedly inhibited the SPAK activity along with mixed-type inhibition against the arginine substrate and noncompetitive inhibition against the ATP cofactor. Spectrofluorimetry results showed that Cu(2+) induced a tertiary structure change in SPAK, resulting in exposure of the hydrophobic surface and increased aggregation. Cu(2+)-mediated SPAK aggregation followed first-order kinetics consistent with monophasic and a biphasic processes. Addition of osmolytes, including glycine and proline, effectively blocked SPAK aggregation and restored SPAK activity. Our results demonstrated the effects of Cu(2+) on SPAK catalytic function, conformation, and aggregation, as well as the protective effects of osmolytes on SPAK folding. This study provided important insights into the role of Cu(2+) as a negative effector of the S. pharaonis metabolic enzyme AK and the possible responses of cephalopods to unfavorable environmental conditions.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Shi XY,Zhang LL,Wu F,Fu YY,Yin SJ,Si YX,Park YDdoi
10.1016/j.ijbiomac.2016.06.049subject
Has Abstractpub_date
2016-10-01 00:00:00pages
926-33eissn
0141-8130issn
1879-0003pii
S0141-8130(16)30587-6journal_volume
91pub_type
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