Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Fang, T.; Tian, Y.; Yuan, S.; Sheng, Y.; Arnesano, F.; Natile, G.; Liu, Y.
    Differential reactivity of metal binding domains of copper ATPases towards cisplatin and colocalization of copper and platinum (2018), Chemistry, 24, 8999-9003 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.2.2.8 expression in Escherichia coli Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.2.2.8 cisplatin comparison of different metal-binding domains of ATPases based on their reactivity towards cisplatin. The rate of platination is generally greater for holo-metal-binding domains than for apo-metal-binding domains. The platinum binding weakens the CuI coordination, but does not expel the copper ion from metal-binding domains; comparison of different metal-binding domains of ATPases based on their reactivity towards cisplatin. The rate of platination is generally greater for holo-metal-binding domains than for apo-metal-binding domains. The platinum binding weakens the CuI coordination, but does not expel the copper ion from metal-binding domains Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
7.2.2.8 Homo sapiens P35670
-
-
7.2.2.8 Homo sapiens Q04656
-
-

Synonyms

EC Number Synonyms Comment Organism
7.2.2.8 ATP7A
-
Homo sapiens
7.2.2.8 ATP7B
-
Homo sapiens
7.2.2.8 Menke's disease protein
-
Homo sapiens
7.2.2.8 Wilson disease protein
-
Homo sapiens