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Literature summary for 4.3.2.2 extracted from
- 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.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli DH5alphaF'IQ cells as recombinant maltose binding protein-ADSL fusion protein | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide | Homo sapiens | - |
5-aminoimidazole-4-carboxamide ribonucleotide + fumarate | - |
? |  |
| succinyladenosine monophosphate | Homo sapiens | - |
AMP + fumarate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P30566 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide | - |
Homo sapiens | 5-aminoimidazole-4-carboxamide ribonucleotide + fumarate | - |
? | |
| succinyladenosine monophosphate | - |
Homo sapiens | AMP + fumarate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homotetramer | - |
Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ADSL | - |
Homo sapiens |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
at 50°C the wild type enzyme shows 79-84% of the activity at 25°C | Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
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