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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
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Tm-value is 39.4°C compared to 46.4°C for wild-type enzyme
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C149S
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loss of zinc content and of enzymic activity
C152S
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loss of zinc content and of enzymic activity
I28V/I118V/I173V
lower temperature stability than wild-type enzyme
F137W
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mutation in domain that closes over the ATP binding site
F86W
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mutation in AMP binding site
P87S
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thermosensitive enzyme, about 50% of wild type activity
S129F
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about 25% of wild type activity
S41W
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mutation in domain that closes over the AMP binding site
Y133W
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mutation in domain that closes over the ATP binding site
P17G
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alters distribution of multiple conformations, lowered secondary structure content, poorer affinity to substrates, reduced catalytic efficiency
P17V
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alters distribution of multiple conformations, lowered secondary structure content, poorer affinity to substrates, reduced catalytic efficiency
C40V
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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
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the mutation is associated with reticular dysgenesis
E9X
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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
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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
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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
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the mutation is associated with reticular dysgenesis
M1V
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the mutation is associated with reticular dysgenesis
R103W
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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
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the mutation is associated with reticular dysgenesis
R7G
when the amino acid residue is mutated, the protein is imported in mitochondria
S1202R
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mutation of RAD50 signature motif, 10-50% of wild-type activity in formation of ADP, formation of ATP is not affected
S231D
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the mutation is associated with reticular dysgenesis
Y152T
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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
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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
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catalytically dead but properly folded variant
K13Q
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catalytically dead but properly folded variant
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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
S1205R
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mutation of RAD50 signature motif, 5-10% of wild-type activity in formation of ADP, formation of ATP is not affected. Complete loss of spore viability in the wild-type/S1205R heterozygote
S1205R
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mutation in Rad50 protein, mutant protein is expressed in yeast and forms a complete complex with Mre11. Mutant does not support spore viability. telomeres are as severely shortened as in a rad50 deletion strain
additional information
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T-DNA insertion mutant. Developing siliques of heterozygous parents contain approximately 25% pale and approximately 75% green seeds. Embryos dissected out of these seeds have a pale green to white color, whitish embryos are homozygous amk2 mutants. Homozygous amk2 seedlings are bleached and strongly retarded in growth. Amk2 heterozygous plants show significantly reduced expression of genes involved in purine de novo synthesis such as PurA, PurB, PurC, PurL, and PurM. Total adenylate kinase activity is reduced by 21% in for ATP formation and 37% for ADP formation
additional information
T-DNA insertion mutant. Developing siliques of heterozygous parents contain approximately 25% pale and approximately 75% green seeds. Embryos dissected out of these seeds have a pale green to white color, whitish embryos are homozygous amk2 mutants. Homozygous amk2 seedlings are bleached and strongly retarded in growth. Amk2 heterozygous plants show significantly reduced expression of genes involved in purine de novo synthesis such as PurA, PurB, PurC, PurL, and PurM. Total adenylate kinase activity is reduced by 21% in for ATP formation and 37% for ADP formation
additional information
T-DNA insertion mutant. Developing siliques of heterozygous parents contain approximately 25% pale and approximately 75% green seeds. Embryos dissected out of these seeds have a pale green to white color, whitish embryos are homozygous amk2 mutants. Homozygous amk2 seedlings are bleached and strongly retarded in growth. Amk2 heterozygous plants show significantly reduced expression of genes involved in purine de novo synthesis such as PurA, PurB, PurC, PurL, and PurM. Total adenylate kinase activity is reduced by 21% in for ATP formation and 37% for ADP formation
additional information
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T-DNA insertion mutants show no phenotype, but significantly increased expression of genes involved in adenine salvage such as Apt1 to Apt5, and Adk1 and Adk2. Also, the PRS genes, responsible for supplying phosphoribosyl diphosphate are significantly induced. 2.5fold increase in expression of isoform Amk2
additional information
T-DNA insertion mutants show no phenotype, but significantly increased expression of genes involved in adenine salvage such as Apt1 to Apt5, and Adk1 and Adk2. Also, the PRS genes, responsible for supplying phosphoribosyl diphosphate are significantly induced. 2.5fold increase in expression of isoform Amk2
additional information
T-DNA insertion mutants show no phenotype, but significantly increased expression of genes involved in adenine salvage such as Apt1 to Apt5, and Adk1 and Adk2. Also, the PRS genes, responsible for supplying phosphoribosyl diphosphate are significantly induced. 2.5fold increase in expression of isoform Amk2
additional information
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construction of chimera between the mesophilic Bacillus subtilis enzyme and the thermophilic Bacillus stearothermophilus enzyme by exchange of one or more of the seven protein segments. Analysis of the chimeras shows spatial separation of stability and activity control with specific contributions of dynamics to catalysis
additional information
no functional complemetation of temperature-sensitive Escherichia coli mutant by concomitant expression of isolated N-terminus, amino acids 1-76 and C-terminus, amino acids 77-217. Weak complementation after fusion with polypeptides that strongly associate
additional information
construction of chimeric adenylate kinase mutants designed by local structural entropy optimization and structure-guided mutagenesis. Generation of LSE-optimized AK variant (AKlse, formerly known as AKlse4) by substituting residues from a mesophilic Bacillus subtilis AKmeso with those of psychrophilic Bacillus globisporus and thermophilic Geobacillus stearothermophilus AKs, AKpsycrho and AKthermo, respectively. Using this AKlse as a template, two additional stable AK mutants, AKm1 and AKm2, formerly known as AKlse4m1 and AKlse4m2, respectively, are generated. Mutant crystals structures analysis, detailed overview
additional information
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construction of chimeric adenylate kinase mutants designed by local structural entropy optimization and structure-guided mutagenesis. Generation of LSE-optimized AK variant (AKlse, formerly known as AKlse4) by substituting residues from a mesophilic Bacillus subtilis AKmeso with those of psychrophilic Bacillus globisporus and thermophilic Geobacillus stearothermophilus AKs, AKpsycrho and AKthermo, respectively. Using this AKlse as a template, two additional stable AK mutants, AKm1 and AKm2, formerly known as AKlse4m1 and AKlse4m2, respectively, are generated. Mutant crystals structures analysis, detailed overview
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additional information
treatment with RNAi results in the suppression of growth of the worm
additional information
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treatment with RNAi results in the suppression of growth of the worm
additional information
construction of chimeric adenylate kinase mutants designed by local structural entropy optimization and structure-guided mutagenesis. Generation of LSE-optimized AK variant (AKlse, formerly known as AKlse4) by substituting residues from a mesophilic Bacillus subtilis AKmeso with those of psychrophilic Bacillus globisporus and thermophilic Geobacillus stearothermophilus AKs, AKpsycrho and AKthermo, respectively. Using this AKlse as a template, two additional stable AK mutants, AKm1 and AKm2, formerly known as AKlse4m1 and AKlse4m2, respectively, are generated. Mutant crystals structures analysis, detailed overview
additional information
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in adenylate kinase knock-out mice, the stimulatory effect of AMP on K/ATP channels is much less pronounced, though not completely suppressed
additional information
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knock out of the major isoform adenylate kinase 1 disrupts the synchrony between inorganic phosphate turnover at ATP-consuming sites and gamma-ATP exchange at ATP synthesis sites. This reduces energetic signal communication in the post-ischemic heart. Adenylate kinase 1 gene deletion blunts vascular adenylate kinase phosphotransfer, compromises the contractility-coronary flow relationship, and precipitates inadequate coronary reflow following ischemiareperfusion. Deficit in adenylate kinase activity abrogates AMP signal generation and reduces the vascular adenylate kinase/creatine kinase activity ratio essential for the response of metabolic sensors. The sarcolemma-associated splice variant adenylate kinase 1beta facilitates adenosine production. Adenosine treatment bypasseds adenylate kinase 1 deficiency and restores post-ischemic flow to wild-type levels
additional information
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knock-down of adenylate kinase 1 results in block of synthesis of external ATP
additional information
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modification of C25 with fluorescent probe IAEDANS, studies of conformatinal changes
additional information
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transgenic plants containing a construct with an antisense fragment of the plastidial adenylate kinase gene. Decreased expression in growing tubers leads to increased rates of respiratory oxygen consumption and increased carbon fluxes into starch. Increased rates of starch synthesis are accompanied by post-translational redox-activation of ADP-glucose diphosphorylase, while there are no substantial changes in metabolic intermediates or sugar levels
additional information
construction of chimeric adenylate kinase mutants designed by local structural entropy optimization and structure-guided mutagenesis. Generation of LSE-optimized AK variant (AKlse, formerly known as AKlse4) by substituting residues from a mesophilic Bacillus subtilis AKmeso with those of psychrophilic Bacillus globisporus and thermophilic Geobacillus stearothermophilus AKs, AKpsycrho and AKthermo, respectively. Using this AKlse as a template, two additional stable AK mutants, AKm1 and AKm2, formerly known as AKlse4m1 and AKlse4m2, respectively, are generated. Mutant crystals structures analysis, detailed overview
additional information
construction of a conditional mutant using fucose inducible adk promoter, the D39 fucose-inducible adk strain
additional information
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construction of a conditional mutant using fucose inducible adk promoter, the D39 fucose-inducible adk strain
additional information
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recombinant expression of full-length enzyme and each of its three catalytic domains. No enzymic activity of a sole catalytic domain
additional information
recombinant expression of full-length enzyme and each of its three catalytic domains. No enzymic activity of a sole catalytic domain
additional information
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expression of full-length protein and each of its three catalytic domains in Escherichia coli. Full-length protein displays high catalytic activity, while none of the catalytic domains alone is active.
additional information
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functional complemetation of temperature-sensitive Escherichia coli mutant by concomitant expression of isolated N-terminus, amino acids 179 and C-terminus, amino acids 80220. Reconstituted enzyme has 17fold lower activity compared with full-length native enzyme