EC Number | Cloned (Comment) | Organism |
---|---|---|
2.3.1.37 | recombinant expression of wild-type and mutant enzymes | Mus musculus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.3.1.37 | K221V | random mutagenesis, library screening, the mutation produces a 23fold increased Km for succinyl-CoA and a 97% decrease in kcat/Km for succinyl-CoA. This reduction in the specificity constant does not stem from lower affinity toward succinyl-CoA, since the Kd for succinyl-CoA of K221V is lower than that of the wild-type enzyme. Mutant K221V has a stronger binding affinity for succinyl-CoA compared to the wild-type enzyme. The mutation reduces the rates of quinonoid intermediate II formation and decay | Mus musculus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.3.1.37 | additional information | - |
additional information | kinetics analysis of wild-type and mutant enzymes, single and multiple turnover and stopped flow measurements, substrate protection study, overview | Mus musculus | |
2.3.1.37 | 0.001 | - |
succinyl-CoA | pH 7.5, 37°C, wild-type enzyme | Mus musculus | |
2.3.1.37 | 0.023 | - |
succinyl-CoA | pH 7.5, 37°C, mutant K221V | Mus musculus | |
2.3.1.37 | 8 | - |
glycine | pH 7.5, 37°C, wild-type enzyme | Mus musculus | |
2.3.1.37 | 50 | - |
glycine | pH 7.5, 37°C, mutant K221V | Mus musculus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.37 | succinyl-CoA + glycine | Mus musculus | - |
5-aminolevulinate + CoA + CO2 | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.1.37 | Mus musculus | P08680 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.3.1.37 | recombinant wild-type and mutant enzymes | Mus musculus |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
2.3.1.37 | succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2 | proposed chemical mechanism of enzyme ALAS2. via (I) internal aldimine complex, (II) glycine-external aldimine, (III) quinonoid intermediate I, (IV) glycinesuccinyl-CoA condensation intermediate, (V) 2-amino-3-ketoadipate intermediate, (VI) enol intermediate, (VII) quinonoid intermediate II, and (VIII) 5-aminolevulinate-external aldimine | Mus musculus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.37 | succinyl-CoA + glycine | - |
Mus musculus | 5-aminolevulinate + CoA + CO2 | - |
r | |
2.3.1.37 | succinyl-CoA + glycine | it is the CoA, rather than the succinyl moiety, that facilitates binding of succinyl-CoA to wild-type ALAS | Mus musculus | 5-aminolevulinate + CoA + CO2 | - |
r |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.3.1.37 | homodimer | the individual active sites are located at the dimeric interface and are composed of amino acids from each subunit | Mus musculus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.3.1.37 | ALAS2 | - |
Mus musculus |
2.3.1.37 | erythroid 5-aminolevulinate synthase | - |
Mus musculus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.3.1.37 | 37 | - |
assay at | Mus musculus |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.3.1.37 | 0.17 | - |
succinyl-CoA | pH 7.5, 37°C, mutant K221V | Mus musculus | |
2.3.1.37 | 0.25 | - |
succinyl-CoA | pH 7.5, 37°C, wild-type enzyme | Mus musculus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.3.1.37 | 7.5 | - |
assay at | Mus musculus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.3.1.37 | pyridoxal 5'-phosphate | dependent on | Mus musculus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.3.1.37 | metabolism | 5-aminolevulinate synthase catalyzs the initial step of mammalian heme biosynthesis | Mus musculus |
2.3.1.37 | additional information | the adenosyl-binding site Lys221 contributes to binding and orientation of succinyl-CoA for effective catalysis | Mus musculus |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.3.1.37 | 7 | - |
succinyl-CoA | pH 7.5, 37°C, mutant K221V | Mus musculus | |
2.3.1.37 | 250 | - |
succinyl-CoA | pH 7.5, 37°C, wild-type enzyme | Mus musculus |