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Literature summary extracted from

  • Randak, C.O.; Dong, Q.; Ver Heul, A.R.; Elcock, A.H.; Welsh, M.J.
    ATP and AMP mutually influence their interaction with the ATP-binding cassette (ABC) adenylate kinase cystic fibrosis transmembrane conductance regulator (CFTR) at separate binding sites (2013), J. Biol. Chem., 288, 27692-27701.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.4.3 wild-type and mutant CFTR are transiently expressed in HeLa cell membranes a double vaccinia virus/T7 RNA polymerase system Homo sapiens
5.6.1.6 transient expression of either wild-type or mutant enzymes in HeLa cell membranes using a vaccinia virus/T7 RNA polymerase expression system Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
5.6.1.6 A462F site-directed mutagenesis, the mutation abolishes nucleotide interaction with ATP-binding site 1, the mutant exhibits a low, ATP-dependent open probability due to a reduced opening rate with a normal burst duration. The A462F mutation interfers with processing and trafficking to the cell membrane Homo sapiens
5.6.1.6 D1370N site-directed mutagenesis of a conserved residue in the Walker B motif of ATP-binding site 2, the mutation abolishes P1,P5-di(adenosine-5') pentaphosphate, Ap5A, inhibition of current Homo sapiens
5.6.1.6 D572N site-directed mutagenesis of a conserved residue in the Walker B motif of ATP-binding site 1, the mutation does not abolish P1,P5-di(adenosine-5') pentaphosphate, Ap5A, inhibition of current Homo sapiens
5.6.1.6 K1250A site-directed mutagenesis of a conserved residue in the Walker A motif of ATP-binding site 2, the mutation abolishes P1,P5-di(adenosine-5') pentaphosphate, Ap5A, inhibition of current Homo sapiens
5.6.1.6 K464A site-directed mutagenesis of a conserved residue in the Walker A motif of ATP-binding site 1, the mutation does not abolish P1,P5-di(adenosine-5') pentaphosphate, Ap5A, inhibition of current Homo sapiens
5.6.1.6 additional information photolabeling of CFTR with 8-N3-[32P]AMP or 8-N3-[32P]ATP Homo sapiens
5.6.1.6 S1248F site-directed mutagenesis, the mutation abolishes nucleotide interaction with ATP-binding site 2, the mutant exhibits a low, ATP-dependent open probability due to a reduced opening rate with a normal burst duration. The S1248F mutation does not interfere with processing and trafficking to the cell membrane Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.4.3 P1,P4-di(adenosine-5') tetraphosphate Ap4A Homo sapiens
2.7.4.3 P1,P5-di(adenosine-5') pentaphosphate Ap5A, interacts simultaneously with an AMP-binding site and ATP-binding site 2 Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
5.6.1.6 membrane
-
 Homo sapiens 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.4.3 Mg2+ required Homo sapiens
5.6.1.6 Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.4.3 ATP + AMP Homo sapiens
-
 2 ADP
-
 r
2.7.4.3 additional information Homo sapiens the cystic fibrosis transmembrane conductance regulator (CFTR) has adenylate kinase activity as an ABC adenylate kinase. ATP enables CFTR photolabeling by 8-N3-AMP, and AMP increases 8-N3-ATP photolabeling at ATP-binding site 2. AMP interacts with CFTR in an ATP-dependent manner and alters ATP interaction with the adenylate kinase active center ATP-binding site. Two other ABC proteins, Rad50 and a structural maintenance of chromosome protein, also have adenylate kinase activity. All three ABC adenylate kinases bind and hydrolyze ATP in the absence of other nucleotides ?
-
 ?
5.6.1.6 ATP + H2O + closed Cl- channel Homo sapiens
-
 ADP + phosphate + open Cl- channel
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.4.3 Homo sapiens
-
-
-
5.6.1.6 Homo sapiens P13569
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.4.3 ATP + AMP
-
 Homo sapiens 2 ADP
-
 r
2.7.4.3 additional information the cystic fibrosis transmembrane conductance regulator (CFTR) has adenylate kinase activity as an ABC adenylate kinase. ATP enables CFTR photolabeling by 8-N3-AMP, and AMP increases 8-N3-ATP photolabeling at ATP-binding site 2. AMP interacts with CFTR in an ATP-dependent manner and alters ATP interaction with the adenylate kinase active center ATP-binding site. Two other ABC proteins, Rad50 and a structural maintenance of chromosome protein, also have adenylate kinase activity. All three ABC adenylate kinases bind and hydrolyze ATP in the absence of other nucleotides Homo sapiens ?
-
 ?
5.6.1.6 ATP + H2O + closed Cl- channel
-
 Homo sapiens ADP + phosphate + open Cl- channel
-
 ?
5.6.1.6 additional information in the presence of ATP and physiologically relevant concentrations of AMP, the enzyme exhibits adenylate kinase activity, converting ATP and AMP into 2 ADP and vice versa. The interaction of nucleotide triphosphate with the enzyme at ATP-binding site 2 is required for this activity. ATP and AMP interact with separate binding sites but mutually influence their interaction with the ABC adenylate kinase CFTR, the active center of the adenylate kinase comprises ATP-binding site 2 Homo sapiens ?
-
 ?

Subunits

EC Number Subunits Comment Organism
5.6.1.6 More construction of a putative molecular three-dimensional model of the nucleotide-binding domain 1-nucleotide-binding domain 2 heterodimer Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
2.7.4.3 ABC adenylate kinase
-
 Homo sapiens
5.6.1.6 CFTR
-
 Homo sapiens
5.6.1.6 cystic fibrosis transmembrane conductance regulator
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.6.1.6 23 26 assay at room temperature Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.4.3 7.5
-
 assay at Homo sapiens
5.6.1.6 7.3
-
 assay at Homo sapiens

General Information

EC Number General Information Comment Organism
2.7.4.3 additional information ATP and AMP interact with separate binding sites but mutually influence their interaction with the ABC adenylate kinase CFTR. The active center of an adenylate kinase comprises separate ATP- and AMP-binding sites, and comprises ATP-binding site 2. Construction of a three-dimensional model of the CFTR NBD1-NBD2 heterodimer, molecular modelling with bound ATP molecules, overview Homo sapiens
5.6.1.6 evolution the enzyme is an ATP-binding cassette (ABC) adenylate kinase and anion channel in the ATP-binding cassette (ABC) transporter protein family Homo sapiens
5.6.1.6 additional information photolabeling of CFTR with 8-N3-[32P]AMP or 8-N3-[32P]ATP, with a photoactivatable azido (N3)-group attached to the adenine ring, the photolabeling is enhanced by AMP and inhibited by P1,P4-di(adenosine-5') tetraphosphate and P1,P5-di(adenosine-5') pentaphosphate, which do not interact with all CFTR ATP-binding sites. Specific labeling of an AMP-binding site in the presence of ATP. Construction of a putative molecular three-dimensional model of the nucleotide-binding domain 1-nucleotide-binding domain 2 heterodimer, the crystal structure of NBD1 in complex with ATP (PDB code 1R0X) is used as template for constructing a homology model of NBD2 Homo sapiens
5.6.1.6 physiological function the enzyme is an ATP-binding cassette adenylate kinase and anion channel Homo sapiens