BRENDA - Enzyme Database

Disease-associated mutations inactivate AMP-lysine hydrolase activity of aprataxin

Seidle, H.F.; Bieganowski, P.; Brenner, C.; J. Biol. Chem. 280, 20927-20931 (2005)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
3.1.11.7
expression in Escherichia coli
Homo sapiens
3.1.11.8
expression in Escherichia coli
Homo sapiens
Engineering
EC Number
Amino acid exchange
Commentary
Organism
3.1.11.7
689insT
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.7
840delT
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.7
A198V
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.7
D267G
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.7
H260A
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.7
K197Q
recessive mutation associated with ataxia but not oculomotor apraxia, mild presentation allele
Homo sapiens
3.1.11.7
P206L
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.7
R199H
recessive mutation associated with ataxia and oculomotor apraxia, protein retains substantial function, consistent with altered activity
Homo sapiens
3.1.11.7
V263G
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.7
W279R
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.7
W279X
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.8
689insT
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.8
840delT
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.8
A198V
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.8
D267G
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.8
H260A
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.8
K197Q
recessive mutation associated with ataxia but not oculomotor apraxia, mild presentation allele
Homo sapiens
3.1.11.8
P206L
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.8
R199H
recessive mutation associated with ataxia and oculomotor apraxia, protein retains substantial function, consistent with altered activity
Homo sapiens
3.1.11.8
V263G
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.8
W279R
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.8
W279X
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.1.11.7
0.021
-
P1,P3-bis(5'-adenosyl)triphosphate
pH 7.2, 22°C
Homo sapiens
3.1.11.7
0.039
-
P1,P4-bis(5'-adenosyl)tetraphosphate
pH 7.2, 22°C
Homo sapiens
3.1.11.8
0.0131
-
Gppp-BODIPY
pH 7.2, 22°C
Homo sapiens
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
3.1.11.7
Homo sapiens
Q7Z2E3
-
-
3.1.11.8
Homo sapiens
Q7Z2E3
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.1.11.7
additional information
aprataxin possesses an active-site-dependent AMP-lysine and GMP-lysine hydrolase activity that depends additionally on the zinc finger for protein stability and on the forkhead associated domain for enzymatic activity. Aprataxin also shows guanosine-5'-diphospho-5'-[DNA] diphosphatase activity, reaction of EC 3.1.11.8
740677
Homo sapiens
?
-
-
-
-
3.1.11.7
P1,P3-bis(5'-adenosyl)triphosphate + H2O
-
740677
Homo sapiens
AMP + ADP
-
-
-
?
3.1.11.7
P1,P4-bis(5'-adenosyl)tetraphosphate + H2O
-
740677
Homo sapiens
?
-
-
-
?
3.1.11.8
Gppp-BODIPY + H2O
-
740677
Homo sapiens
?
-
-
-
?
3.1.11.8
additional information
aprataxin possesses an active-site-dependent AMP-lysine and GMP-lysine hydrolase activity that depends additionally on the zinc finger for protein stability and on the forkhead associated domain for enzymatic activity. Aprataxin also shows adenosine-5'-diphospho-5'-[DNA] diphosphatase activity, reaction of EC 3.1.11.7
740677
Homo sapiens
?
-
-
-
-
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
3.1.11.7
0.00008
-
P1,P3-bis(5'-adenosyl)triphosphate
pH 7.2, 22°C
Homo sapiens
3.1.11.7
0.0009
-
P1,P4-bis(5'-adenosyl)tetraphosphate
pH 7.2, 22°C
Homo sapiens
3.1.11.8
0.0004
-
Gppp-BODIPY
pH 7.2, 22°C
Homo sapiens
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
3.1.11.7
expression in Escherichia coli
Homo sapiens
3.1.11.8
expression in Escherichia coli
Homo sapiens
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
3.1.11.7
689insT
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.7
840delT
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.7
A198V
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.7
D267G
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.7
H260A
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.7
K197Q
recessive mutation associated with ataxia but not oculomotor apraxia, mild presentation allele
Homo sapiens
3.1.11.7
P206L
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.7
R199H
recessive mutation associated with ataxia and oculomotor apraxia, protein retains substantial function, consistent with altered activity
Homo sapiens
3.1.11.7
V263G
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.7
W279R
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.7
W279X
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.8
689insT
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.8
840delT
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.8
A198V
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.8
D267G
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.8
H260A
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.8
K197Q
recessive mutation associated with ataxia but not oculomotor apraxia, mild presentation allele
Homo sapiens
3.1.11.8
P206L
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.8
R199H
recessive mutation associated with ataxia and oculomotor apraxia, protein retains substantial function, consistent with altered activity
Homo sapiens
3.1.11.8
V263G
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.8
W279R
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
3.1.11.8
W279X
recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability
Homo sapiens
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.1.11.7
0.021
-
P1,P3-bis(5'-adenosyl)triphosphate
pH 7.2, 22°C
Homo sapiens
3.1.11.7
0.039
-
P1,P4-bis(5'-adenosyl)tetraphosphate
pH 7.2, 22°C
Homo sapiens
3.1.11.8
0.0131
-
Gppp-BODIPY
pH 7.2, 22°C
Homo sapiens
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.1.11.7
additional information
aprataxin possesses an active-site-dependent AMP-lysine and GMP-lysine hydrolase activity that depends additionally on the zinc finger for protein stability and on the forkhead associated domain for enzymatic activity. Aprataxin also shows guanosine-5'-diphospho-5'-[DNA] diphosphatase activity, reaction of EC 3.1.11.8
740677
Homo sapiens
?
-
-
-
-
3.1.11.7
P1,P3-bis(5'-adenosyl)triphosphate + H2O
-
740677
Homo sapiens
AMP + ADP
-
-
-
?
3.1.11.7
P1,P4-bis(5'-adenosyl)tetraphosphate + H2O
-
740677
Homo sapiens
?
-
-
-
?
3.1.11.8
Gppp-BODIPY + H2O
-
740677
Homo sapiens
?
-
-
-
?
3.1.11.8
additional information
aprataxin possesses an active-site-dependent AMP-lysine and GMP-lysine hydrolase activity that depends additionally on the zinc finger for protein stability and on the forkhead associated domain for enzymatic activity. Aprataxin also shows adenosine-5'-diphospho-5'-[DNA] diphosphatase activity, reaction of EC 3.1.11.7
740677
Homo sapiens
?
-
-
-
-
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
3.1.11.7
0.00008
-
P1,P3-bis(5'-adenosyl)triphosphate
pH 7.2, 22°C
Homo sapiens
3.1.11.7
0.0009
-
P1,P4-bis(5'-adenosyl)tetraphosphate
pH 7.2, 22°C
Homo sapiens
3.1.11.8
0.0004
-
Gppp-BODIPY
pH 7.2, 22°C
Homo sapiens
KCat/KM [mM/s]
EC Number
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
3.1.11.7
0.0038
-
P1,P3-bis(5'-adenosyl)triphosphate
pH 7.2, 22°C
Homo sapiens
3.1.11.7
0.023
-
P1,P4-bis(5'-adenosyl)tetraphosphate
pH 7.2, 22°C
Homo sapiens
3.1.11.8
0.031
-
Gppp-BODIPY
pH 7.2, 22°C
Homo sapiens
KCat/KM [mM/s] (protein specific)
EC Number
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
3.1.11.7
0.0038
-
P1,P3-bis(5'-adenosyl)triphosphate
pH 7.2, 22°C
Homo sapiens
3.1.11.7
0.023
-
P1,P4-bis(5'-adenosyl)tetraphosphate
pH 7.2, 22°C
Homo sapiens
3.1.11.8
0.031
-
Gppp-BODIPY
pH 7.2, 22°C
Homo sapiens