General Stability | Organism |
---|---|
short half-life | Gallus gallus |
short half-life | Mus musculus |
short half-life | Homo sapiens |
short half-life | Rattus norvegicus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
protoheme | feed-back inhibition, non-specific isoform ALAS-1 | Gallus gallus | |
protoheme | feed-back inhibition, non-specific isoform ALAS-1 | Homo sapiens | |
protoheme | feed-back inhibition, non-specific isoform ALAS-1 | Mus musculus | |
protoheme | feed-back inhibition, non-specific isoform ALAS-1 | Rattus norvegicus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.055 | - |
succinyl-CoA | - |
Mus musculus | |
51 | - |
glycine | - |
Mus musculus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Iron | regulation of erythroid-specific isoform ALAS-2 via 5'-iron responsive element, i.e. IRE | Gallus gallus | |
Iron | regulation of erythroid-specific isoform ALAS-2 via 5'-iron responsive element, i.e. IRE | Mus musculus | |
Iron | regulation of erythroid-specific isoform ALAS-2 via 5'-iron responsive element, i.e. IRE | Homo sapiens | |
Iron | regulation of erythroid-specific isoform ALAS-2 via 5'-iron responsive element, i.e. IRE | Rattus norvegicus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
56000 | - |
2 * 56000, SDS-PAGE | Mus musculus |
112000 | - |
gel filtration | Mus musculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Homo sapiens | enzyme deficiency causes X-linked sideroblastic anemia | ? | - |
? | |
succinyl-CoA + glycine | Gallus gallus | key enzyme in tetrapyrrole biosynthesis | 5-aminolevulinate + CoA + CO2 | - |
? | |
succinyl-CoA + glycine | Mus musculus | key enzyme in tetrapyrrole biosynthesis | 5-aminolevulinate + CoA + CO2 | - |
? | |
succinyl-CoA + glycine | Homo sapiens | key enzyme in tetrapyrrole biosynthesis | 5-aminolevulinate + CoA + CO2 | - |
? | |
succinyl-CoA + glycine | Rattus norvegicus | key enzyme in tetrapyrrole biosynthesis | 5-aminolevulinate + CoA + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Gallus gallus | - |
2 isoforms ALAS-1 and ALAS-2, a houskeeping form and an erythroid-specific form | - |
Homo sapiens | - |
2 isoforms ALAS-1 and ALAS-2, a houskeeping form and an erythroid-specific form | - |
Mus musculus | - |
2 isoforms ALAS-1 and ALAS-2, a houskeeping form and an erythroid-specific form | - |
Rattus norvegicus | - |
non-specific, housekeeping isoform ALAS-N and erythroid-specific isoform ALAS-E | - |
Purification (Comment) | Organism |
---|---|
recombinant from E. coli | Mus musculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
additional information | enzyme is synthezised in the cytosol as the precursor protein and then imported into the mitochondria matrix and cleaved to the mature enzyme, the targeting information is encoded in nonoverlapping regions of the presequence | Gallus gallus | - |
additional information | enzyme is synthezised in the cytosol as the precursor protein and then imported into the mitochondria matrix and cleaved to the mature enzyme, the targeting information is encoded in nonoverlapping regions of the presequence | Mus musculus | - |
additional information | enzyme is synthezised in the cytosol as the precursor protein and then imported into the mitochondria matrix and cleaved to the mature enzyme, the targeting information is encoded in nonoverlapping regions of the presequence | Homo sapiens | - |
additional information | enzyme is synthezised in the cytosol as the precursor protein and then imported into the mitochondria matrix and cleaved to the mature enzyme, the targeting information is encoded in nonoverlapping regions of the presequence | Rattus norvegicus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | enzyme deficiency causes X-linked sideroblastic anemia | Homo sapiens | ? | - |
? | |
succinyl-CoA + glycine | - |
Gallus gallus | 5-aminolevulinate + CoA + CO2 | - |
? | |
succinyl-CoA + glycine | - |
Mus musculus | 5-aminolevulinate + CoA + CO2 | - |
? | |
succinyl-CoA + glycine | - |
Homo sapiens | 5-aminolevulinate + CoA + CO2 | - |
? | |
succinyl-CoA + glycine | - |
Rattus norvegicus | 5-aminolevulinate + CoA + CO2 | - |
? | |
succinyl-CoA + glycine | key enzyme in tetrapyrrole biosynthesis | Gallus gallus | 5-aminolevulinate + CoA + CO2 | - |
? | |
succinyl-CoA + glycine | key enzyme in tetrapyrrole biosynthesis | Mus musculus | 5-aminolevulinate + CoA + CO2 | - |
? | |
succinyl-CoA + glycine | key enzyme in tetrapyrrole biosynthesis | Homo sapiens | 5-aminolevulinate + CoA + CO2 | - |
? | |
succinyl-CoA + glycine | key enzyme in tetrapyrrole biosynthesis | Rattus norvegicus | 5-aminolevulinate + CoA + CO2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | - |
Gallus gallus |
dimer | - |
Rattus norvegicus |
dimer | 2 * 56000, SDS-PAGE | Mus musculus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0095 | - |
succinyl-CoA | - |
Mus musculus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | required | Gallus gallus | |
pyridoxal 5'-phosphate | required | Mus musculus | |
pyridoxal 5'-phosphate | required | Homo sapiens | |
pyridoxal 5'-phosphate | required | Rattus norvegicus | |
pyridoxal 5'-phosphate | noncovalently bound | Mus musculus |