EC 5 - Isomerases
EC 5.6 - Isomerases altering macromolecular conformation,
EC 5.6.1 - Enzymes altering polypeptide conformation or assembly
EC 5.6.1.6 - Channel-conductance-controlling ATPase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 5.6.1.6
Names
Accepted name:
channel-conductance-controlling ATPase
Other
names:
cystic-fibrosis membrane-conductance-regulating protein
CFTR
CFTR
Systematic name:
ATP phosphohydrolase (channel-conductance-controlling)
Reaction
- ATP + H2O + closed Cl- channel = ADP + phosphate + open Cl- channel
Comments:
ABC-type (ATP-binding cassette-type) ATPase, characterized by the presence of two similar ATP-binding domains. The enzyme is found in animals, and in humans its absence brings about cystic fibrosis. Unlike most of the ABC transporters, chloride pumping is not directly coupled to ATP hydrolysis. Instead, the passive flow of anions through the channel is gated by cycles of ATP binding and hydrolysis by the ATP-binding domains. The enzyme is also involved in the functioning of other transmembrane channels. Formerly EC 3.6.3.49.
Links to other databases
Protein domains and families:
PROSITE:PDOC00185
Gene Ontology:
GO:0005260
References
-
Membrane insertion, processing, and topology of cystic fibrosis transmembrane conductance regulator (CFTR) in microsomal membranes.Mol. Membr. Biol. 13 : 33-40 (1996). [PMID: 9147660]
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Membrane topology distinguishes a subfamily of the ATP-binding cassette (ABC) transporters.FEBS Lett. 402 : 1-3 (1997). [PMID: 9013845]
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Structure and function of the CFTR chloride channel.Physiol. Rev. 79 : S23-S45 (1999). [PMID: 9922375]
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Gating of the CFTR Cl- channel by ATP-driven nucleotide-binding domain dimerisation.J. Physiol. (Lond.) 587 : 2151-2161 (2009). [PMID: 19332488]
[EC 5.6.1.6 created 2000 as EC 3.6.3.49, transferred 2018 to EC 5.6.1.6]