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

BRENDA support

2.7.4.3: adenylate kinase

This is an abbreviated version!
For detailed information about adenylate kinase, go to the full flat file.

Word Map on EC 2.7.4.3

Reaction

ATP
+
AMP
=
2 ADP

Synonyms

5'-AMP-kinase, ABC adenylate kinase, AD-004 like protein, adenosine 5'-triphosphate:adenosine 5'-monophosphate phosphotransferase, adenylate kinase, adenylate kinase 1, adenylate kinase 2, adenylate kinase 4, adenylate kinase 5, adenylate kinase 6, adenylate kinase 9, adenylate kinase isoenzyme 1, adenylate kinase isozyme 2, adenylate kinase-2, adenylate kinase-like protein 1, adenylic kinase, adenylokinase, ADK, ADK1, ADK2, ADLP, AK1, AK2, AK4, AK5, AK5p1, AK5p2, AK6, AK7, AK8, AK9, AKE, AKlse4, AKm, AKmeso, AKp, AKpsycrho, AKthermo, ATP:AMP phosphotransferase, CFTR, CINAP, coilin interacting nuclear ATPase protein, cystic fibrosis transmembrane conductance regulator, DAK2, Dak6, kinase, adenylate (phosphorylating), kinase, myo- (phosphorylating), MeADK1, MeADK2, MJ0458, myokinase, nonstructural protein 4B, NS4B, pfSMCnbd, phosphotransferase, Rv0733, Saci_0573, SpAdK, structural maintenance of chromosome protein

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.4 Phosphotransferases with a phosphate group as acceptor
                2.7.4.3 adenylate kinase

Engineering

Engineering on EC 2.7.4.3 - adenylate kinase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
I26T
Tm-value is 39.4°C compared to 46.4°C for wild-type enzyme
Q16L/Q199R
thermostabilization of full-length protein. Cells harboring the mutant fragment pair with concomitant expression of isolated N-terminus, amino acids 1-76 and C-terminus, amino acids 77-217 show weak complementation of Escherichia coli mutant after fusion with polypeptides that strongly associate
Q199R
modest increase in stability, 3 degrees increase in melting temperature. At temperatures of 20°C to 45°C, 50% loss of activity, with subsequent increase at higher temperatures. rigidification of he overall structure through stabilization of a polypeptide loop containing R199 that is part of the ATP-binding site
I26T
-
Tm-value is 39.4°C compared to 46.4°C for wild-type enzyme
-
C149S
-
loss of zinc content and of enzymic activity
C152S
-
loss of zinc content and of enzymic activity
I28V/I118V/I173V
lower temperature stability than wild-type enzyme
F137W
-
mutation in domain that closes over the ATP binding site
F86W
-
mutation in AMP binding site
P87S
-
thermosensitive enzyme, about 50% of wild type activity
S129F
-
about 25% of wild type activity
S41W
-
mutation in domain that closes over the AMP binding site
Y133W
-
mutation in domain that closes over the ATP binding site
P17G
-
alters distribution of multiple conformations, lowered secondary structure content, poorer affinity to substrates, reduced catalytic efficiency
P17V
-
alters distribution of multiple conformations, lowered secondary structure content, poorer affinity to substrates, reduced catalytic efficiency
C40V
-
the mutation is associated with reticular dysgenesis
D140del
mutation identified in patient deficient in red cell adenylate kinase, suffering from chronic hemolytic anemia. 30% residual adenylate kinase activity
D165G
-
the mutation is associated with reticular dysgenesis
E9X
-
the mutation is associated with reticular dysgenesis
G40R
mutation identified in patient deficient in red cell adenylate kinase, suffering from chronic hemolytic anemia. 25% residual adenylate kinase activity
H79G
the mutation affects both adenylate kinase (enzymatic efficiency (kcat/Km) is reduced by 72% relative to the wild type enzyme) and ATPase catalytic efficiency and induces homodimer formation
K233X
-
the mutation is associated with reticular dysgenesis
K4G
when the amino acid residue is mutated, the protein is imported in mitochondria
K4G/R7G
when both amino acid residues are mutated simultaneously the protein remains in the cytosol
L1254A
-
mutant in cystic fibrosis transmembrane conductance regulator. Cystic fibrosis transmembrane conductance regulator shows adenylate kinase activity in the presence of ATP plus physiologic concentrations of AMP or ADP. P1,P5-di(adenosine-5') pentaphosphate increases the activity of the mutant. The mutation increases the EC50 for ATP by more than 10-fold and reduces channel activity by prolonging the closed state. P1,P5-di(adenosine-5') pentaphosphate changes the relationship between ATP concentration and current. At submaximal ATP concentrations, P1,P5-di(adenosine-5') pentaphosphate stimulates current by stabilizing the channel open state
L171P
the mutation dramatically changes the orientation of the LID domain, which can be described as a twisted and closed conformation in contrast to the open and closed conformations in other adenylate kinases
L183X
-
the mutation is associated with reticular dysgenesis
M1V
-
the mutation is associated with reticular dysgenesis
R103W
-
the mutation is associated with reticular dysgenesis
R128W
mutation identified in patient deficient in red cell adenylate kinase, suffering from chronic hemolytic anemia. 44% residual adenylate kinase activity
R186C
-
the mutation is associated with reticular dysgenesis
R7G
when the amino acid residue is mutated, the protein is imported in mitochondria
S1202R
-
mutation of RAD50 signature motif, 10-50% of wild-type activity in formation of ADP, formation of ATP is not affected
S231D
-
the mutation is associated with reticular dysgenesis
Y152T
-
the mutation is associated with reticular dysgenesis
Y164C
mutation identified in patient deficient in red cell adenylate kinase, suffering from chronic hemolytic anemia. 0% residual adenylate kinase activity
G551D
mutation affects the ability of the nucleotide-binding domain 1 of CFTR to dimerize, has an exaggerated nonlinear phase compared with the wild type
S48A
Tm-value is 36.0°C, compared to 33.8°C for the wild-type enzyme
T188K
Tm-value is 30.7°C, compared to 33.8°C for the wild-type enzyme
V118I
Tm-value is 36.6°C, compared to 33.8°C for the wild-type enzyme
V118I/V173I
Tm-value is 41.4°C, compared to 33.8°C for the wild-type enzyme
V173I
Tm-value is 36.3°C, compared to 33.8°C for the wild-type enzyme
V28I
Tm-value is 38.8°C, compared to 33.8°C for the wild-type enzyme
V28I/V118I/V173I
Tm-value is 45.1°C, compared to 33.8°C for the wild-type enzyme
S793R
-
mutation in Rad50 singature motif. Mutant shows lower levels of both ATPase and adenylate kinase activity relative to the wild-type enzyme, consistent with an overall deficiency in ATP binding
K13Q
-
catalytically dead but properly folded variant
S1205R
K13Q
-
catalytically dead but properly folded variant
-
T26A
the Tm-value is 38.4°C compared to 42.7°C for wild-type enzyme
T26F
the Tm-value is 43.0°C compared to 42.7°C for wild-type enzyme
T26I
the Tm-value is 50.8°C compared to 42.7°C for wild-type enzyme
T26L
the Tm-value is 48.4°C compared to 42.7°C for wild-type enzyme
T26N
the Tm-value is 38.3°C compared to 42.7°C for wild-type enzyme
T26S
the Tm-value is 38.7°C compared to 42.7°C for wild-type enzyme
T26V
the Tm-value is 48.3°C compared to 42.7°C for wild-type enzyme
T26Y
the Tm-value is 44.1°C compared to 42.7°C for wild-type enzyme
R89A
site-directed mutagenesis, inactive active site mutant
additional information