EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
4.2.1.22 | AdoMet | allosteric regulator, 1mol per mole of monomeric subunit activates the enzyme 2fold | Homo sapiens | |
4.2.1.22 | additional information | oxidizing conditions increase the enzyme activity by 2fold | Mammalia |
EC Number | Cloned (Comment) | Organism |
---|---|---|
4.2.1.22 | - |
Homo sapiens |
4.2.1.22 | - |
Saccharomyces cerevisiae |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
4.2.1.22 | C272A | spectroscopic properties similar to wild-type enzyme | Mammalia |
4.2.1.22 | C275S | spectroscopic properties similar to wild-type enzyme | Mammalia |
4.2.1.22 | D444N | high level of enzyme activity | Homo sapiens |
4.2.1.22 | additional information | C-terminal regulatory domain deletion leads to formation of highly active dimeric enzyme | Homo sapiens |
4.2.1.22 | additional information | C-terminal regulatory domain deletion leads to formation of highly active dimeric enzyme | Saccharomyces cerevisiae |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
4.2.1.22 | Dithionite | 2fold decrease in enzyme activity due to altered oxidation state of the heme | Mammalia | |
4.2.1.22 | titanium citrate | 2fold decrease in enzyme activity due to altered oxidation state of the heme | Mammalia |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.2.1.22 | additional information | Mammalia | first step in transsulfuration pathway | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.2.1.22 | Homo sapiens | - |
- |
- |
4.2.1.22 | Mammalia | - |
- |
- |
4.2.1.22 | Saccharomyces cerevisiae | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
4.2.1.22 | L-serine + L-homocysteine = L-cystathionine + H2O | mechanism | Homo sapiens | |
4.2.1.22 | L-serine + L-homocysteine = L-cystathionine + H2O | mechanism | Saccharomyces cerevisiae |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
4.2.1.22 | fibroblast | - |
Homo sapiens | - |
4.2.1.22 | liver | - |
Homo sapiens | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.2.1.22 | L-Serine + homocysteine | - |
Mammalia | Cystathionine + H2O | - |
r | |
4.2.1.22 | L-Serine + homocysteine | - |
Homo sapiens | Cystathionine + H2O | - |
r | |
4.2.1.22 | L-Serine + homocysteine | - |
Saccharomyces cerevisiae | Cystathionine + H2O | - |
r | |
4.2.1.22 | additional information | first step in transsulfuration pathway | Mammalia | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.2.1.22 | dimer | after deletion of the C-terminal regulatory domain | Homo sapiens |
4.2.1.22 | dimer | after deletion of the C-terminal regulatory domain | Saccharomyces cerevisiae |
4.2.1.22 | octamer | homooctamer | Saccharomyces cerevisiae |
4.2.1.22 | tetramer | alpha4 homotetramer | Homo sapiens |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
4.2.1.22 | heme | iron protoporphyrin IX | Mammalia | |
4.2.1.22 | pyridoxal 5'-phosphate | dependent | Mammalia | |
4.2.1.22 | pyridoxal 5'-phosphate | dependent | Homo sapiens | |
4.2.1.22 | pyridoxal 5'-phosphate | dependent | Saccharomyces cerevisiae |