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Literature summary extracted from

  • Zikanova, M.; Skopova, V.; Hnizda, A.; Krijt, J.; Kmoch, S.
    Biochemical and structural analysis of 14 mutant ADSL enzyme complexes and correlation to phenotypic heterogeneity of adenylosuccinate lyase deficiency (2010), Hum. Mutat., 31, 445-455.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.3.2.2 expressed in Escherichia coli DH5alphaF'IQ cells as recombinant maltose binding protein-ADSL fusion protein Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
4.3.2.2 D215H the mutation is associated with ADSL deficiency and shows 92% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme Homo sapiens
4.3.2.2 D268H the mutation is associated with ADSL deficiency and shows 20% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme Homo sapiens
4.3.2.2 D430N the mutation is associated with ADSL deficiency and shows 151% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme Homo sapiens
4.3.2.2 D87E the mutation is associated with ADSL deficiency and shows 91% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme Homo sapiens
4.3.2.2 E376D the mutation is associated with ADSL deficiency and shows 49% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme Homo sapiens
4.3.2.2 E80D the mutation is associated with ADSL deficiency and shows 102% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme Homo sapiens
4.3.2.2 I351T the mutation is associated with ADSL deficiency and shows 151% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme Homo sapiens
4.3.2.2 R190Q the mutation is associated with ADSL deficiency and shows 119% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme Homo sapiens
4.3.2.2 R194C the mutation is associated with ADSL deficiency and shows 101% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme Homo sapiens
4.3.2.2 R396C the mutation is associated with ADSL deficiency and shows 32% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme Homo sapiens
4.3.2.2 R426H the mutation is associated with ADSL deficiency and shows 89% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme Homo sapiens
4.3.2.2 S23R the mutation is associated with ADSL deficiency and shows 108% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme Homo sapiens
4.3.2.2 T242I the mutation is associated with ADSL deficiency and shows 108% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme Homo sapiens
4.3.2.2 T450S the mutation is associated with ADSL deficiency and shows 68% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme Homo sapiens
4.3.2.2 Y114H the mutation is associated with ADSL deficiency and shows 37% activity using 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide as substrate at 25°C compared to the wild type enzyme Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.3.2.2 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide Homo sapiens
-
 5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
 ?
4.3.2.2 succinyladenosine monophosphate Homo sapiens
-
 AMP + fumarate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.3.2.2 Homo sapiens P30566
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.2.2 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
-
 Homo sapiens 5-aminoimidazole-4-carboxamide ribonucleotide + fumarate
-
 ?
4.3.2.2 succinyladenosine monophosphate
-
 Homo sapiens AMP + fumarate
-
 ?

Subunits

EC Number Subunits Comment Organism
4.3.2.2 homotetramer
-
 Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
4.3.2.2 ADSL
-
 Homo sapiens

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.3.2.2 50
-
 at 50°C the wild type enzyme shows 79-84% of the activity at 25°C Homo sapiens

General Information

EC Number General Information Comment Organism
4.3.2.2 malfunction phenotypic severity in ADSL deficiency is correlated with residual enzymatic activity and structural stability of the corresponding mutant ADSL complexes and does not result from genotype-specific disproportional catalytic activities toward one of the enzyme substrates Homo sapiens