EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
4.2.1.22 | additional information | enzyme can not be activated by S-adenosyl-L-methionine | Trypanosoma cruzi | |
4.2.1.22 | S-adenosyl-L-methionine | 3fold activation, allosteric regulator | Saccharomyces cerevisiae | |
4.2.1.22 | S-adenosyl-L-methionine | 3fold activation, allosteric regulator of the full length enzyme, does not activate the truncated enzyme | Homo sapiens |
EC Number | Application | Comment | Organism |
---|---|---|---|
4.2.1.22 | medicine | inherited dysfunction of the enzyme leads to homocystinurea, mutations can occur at the dimer interface, the active site, the heme-binding site and the predicted interface region between the catalytic domain and the missing regulatory domain of the truncated enzyme | Homo sapiens |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
4.2.1.22 | S466L | enzyme is constitutively activated, does bind S-adenosyl-L-methionine, but is not activated by it | Homo sapiens |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.2.1.22 | Homo sapiens | P35520 | - |
- |
4.2.1.22 | Saccharomyces cerevisiae | - |
- |
- |
4.2.1.22 | Trypanosoma cruzi | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
4.2.1.22 | L-serine + L-homocysteine = L-cystathionine + H2O | ping-pong mechanism | Saccharomyces cerevisiae | |
4.2.1.22 | L-serine + L-homocysteine = L-cystathionine + H2O | ping-pong mechanism | Homo sapiens |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
4.2.1.22 | fibroblast | - |
Homo sapiens | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.2.1.22 | L-cysteine + 2-mercaptoethanol | - |
Homo sapiens | S-hydroxyethyl-L-cysteine + H2S | - |
? | |
4.2.1.22 | L-Serine + homocysteine | - |
Saccharomyces cerevisiae | Cystathionine + H2O | - |
r | |
4.2.1.22 | L-Serine + homocysteine | - |
Trypanosoma cruzi | Cystathionine + H2O | - |
r | |
4.2.1.22 | L-Serine + homocysteine | catalyzes a beta-replacement reaction in which an electronegative substituent in the beta-position of the amino acid substrate is replaced by a nucleophile, binding of L-serine as the external aldimine is faster than formation of the aminoacrylate intermediate, the rate-limiting step is the reaction of aminoacrylate with L-homocysteine to form L-cystathione, rate of the forward reaction is 38fold greater than the reverse reaction | Homo sapiens | Cystathionine + H2O | - |
r |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
4.2.1.22 | heme | - |
Homo sapiens | |
4.2.1.22 | additional information | heme is no cofactor | Saccharomyces cerevisiae | |
4.2.1.22 | additional information | heme is no cofactor | Trypanosoma cruzi | |
4.2.1.22 | pyridoxal 5'-phosphate | - |
Saccharomyces cerevisiae | |
4.2.1.22 | pyridoxal 5'-phosphate | - |
Trypanosoma cruzi | |
4.2.1.22 | pyridoxal 5'-phosphate | dependent | Homo sapiens |