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Literature summary for 4.3.2.1 extracted from

  • Hu, L.; Pandey, A.V.; Balmer, C.; Eggimann, S.; Ruefenacht, V.; Nuoffer, J.M.; Haeberle, J.
    Unstable argininosuccinate lyase in variant forms of the urea cycle disorder argininosuccinic aciduria (2015), J. Inherit. Metab. Dis., 38, 815-827 .
    View publication on PubMed
Search for more literature for 4.3.2.1

Cloned(Commentary)

Cloned (Comment) Organism
expression of ASL constructs in human embryonic kidney 293T cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
E189G the mutant enzyme decreased enzyme efficiency (78% of wild-type), no significant decrease in Km-value, displays thermal instability Homo sapiens
I100T the mutant enzyme decreased enzyme efficiency (61% of wild-type), no significant decrease in Km-value, displays thermal instability Homo sapiens
R379C no significant decrease in Km-value, displays thermal instability Homo sapiens
R95C the mutant enzyme decreased enzyme efficiency (32% of wild-type), no significant decrease in Km-value, displays thermal instability Homo sapiens
V178M no significant reduced Km-value, displays thermal instability Homo sapiens
V335L the mutant enzyme decreased enzyme efficiency (48% of wild-type), no significant decrease in Km-value, displays thermal instability Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.18
-
 2-(Nomega-L-arginino)succinate pH 7.5, 37°C, mutant enzyme R95C Homo sapiens
0.25
-
 2-(Nomega-L-arginino)succinate pH 7.5, 37°C, mutant enzyme R379C Homo sapiens
0.44
-
 2-(Nomega-L-arginino)succinate pH 7.5, 37°C, wild-type enzyme Homo sapiens
0.44
-
 2-(Nomega-L-arginino)succinate pH 7.5, 37°C, mutant enzyme V178M Homo sapiens
0.46
-
 2-(Nomega-L-arginino)succinate pH 7.5, 37°C, mutant enzyme I100T Homo sapiens
0.49
-
 2-(Nomega-L-arginino)succinate pH 7.5, 37°C, mutant enzyme E189G Homo sapiens
0.53
-
 2-(Nomega-L-arginino)succinate pH 7.5, 37°C, mutant enzyme V335L Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-(Nomega-L-arginino)succinate Homo sapiens as part of the urea cycle, the enzyme is essential for ammonia detoxification and L-arginine synthesis fumarate + L-arginine
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P04424
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-(Nomega-L-arginino)succinate
-
 Homo sapiens fumarate + L-arginine
-
 ?
2-(Nomega-L-arginino)succinate as part of the urea cycle, the enzyme is essential for ammonia detoxification and L-arginine synthesis Homo sapiens fumarate + L-arginine
-
 ?

Synonyms

Synonyms Comment Organism
ASL
-
 Homo sapiens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
42.4
-
 Tm-value: mutant enzyme V335L Homo sapiens
46.5
-
 Tm-value: mutant enzyme R95C Homo sapiens
48
-
 Tm-value: mutant enzyme R379C Homo sapiens
48.1
-
 Tm-value: mutant enzyme E189G Homo sapiens
48.5
-
 Tm-value: mutant enzyme I100T Homo sapiens
49.9
-
 Tm-value: mutant enzyme V178M Homo sapiens
52.7
-
 Tm-value: wild-type enzyme Homo sapiens

General Information

General Information Comment Organism
malfunction argininosuccinate lyase deficiency (ASLD) is a rare autosomal-recessive urea cycle defect caused by mutations in the ASL gene encoding argininosuccinate lyase. ASLD has a broad clinical spectrum ranging from life-threatening severe neonatal to asymptomatic forms. Different levels of residual ASL activity probably contribute to the phenotypic variability. All ASL mutations that are identified in patients with late onset or mild clinical and biochemical courses by ASL expression in human embryonic kidney are investigated Homo sapiens
metabolism as part of the urea cycle, the enzyme is essential for ammonia detoxification and L-arginine synthesis Homo sapiens
physiological function as part of the urea cycle, the enzyme is essential for ammonia detoxification and L-arginine synthesis Homo sapiens