Literature summary for 5.6.1.6 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.

Search for more literature for 5.6.1.6

Cloned(Commentary)

Cloned (Comment)	Organism
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

Protein Variants	Comment	Organism
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
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
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
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
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
additional information	photolabeling of CFTR with 8-N3-[32P]AMP or 8-N3-[32P]ATP	Homo sapiens
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

Localization

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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + H2O + closed Cl- channel	Homo sapiens	-	ADP + phosphate + open Cl- channel	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P13569	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O + closed Cl- channel	-	Homo sapiens	ADP + phosphate + open Cl- channel	-	?
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

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

Synonyms

Synonyms	Comment	Organism
CFTR	-	Homo sapiens
cystic fibrosis transmembrane conductance regulator	-	Homo sapiens

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.3	-	assay at	Homo sapiens

General Information

General Information	Comment	Organism
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
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
physiological function	the enzyme is an ATP-binding cassette adenylate kinase and anion channel	Homo sapiens

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Release 2023.1 (January 2023)