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Literature summary for 3.6.1.70 extracted from

  • Seidle, H.F.; Bieganowski, P.; Brenner, C.
    Disease-associated mutations inactivate AMP-lysine hydrolase activity of aprataxin (2005), J. Biol. Chem., 280, 20927-20931.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens

Protein Variants

Protein Variants Comment Organism
689insT recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability Homo sapiens
840delT recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability Homo sapiens
A198V recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability Homo sapiens
D267G recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability Homo sapiens
H260A recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability Homo sapiens
K197Q recessive mutation associated with ataxia but not oculomotor apraxia, mild presentation allele Homo sapiens
P206L recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability Homo sapiens
R199H recessive mutation associated with ataxia and oculomotor apraxia, protein retains substantial function, consistent with altered activity Homo sapiens
V263G recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability Homo sapiens
W279R recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability Homo sapiens
W279X recessive mutation associated with ataxia and oculomotor apraxia, huge loss in protein stability Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0131
-
Gppp-BODIPY pH 7.2, 22°C Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q7Z2E3
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Gppp-BODIPY + H2O
-
Homo sapiens ?
-
?
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 Homo sapiens ?
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0004
-
Gppp-BODIPY pH 7.2, 22°C Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.031
-
Gppp-BODIPY pH 7.2, 22°C Homo sapiens