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Literature summary for 4.2.1.22 extracted from
- Trypsin cleavage of human cystathionine beta-synthase into an evolutionary conserved active core: structural and functional consequences (1998), Arch. Biochem. Biophys., 355, 222-232.
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-Serine + homocysteine | Homo sapiens | irreversible step in transsulfuration pathway | ? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | trypsinolyis occurs initially at Lys30, Lys36, Lys39, then at Arg413 and transforms the tetrameric enzyme to a dimer of MW 85000 which is twice as active as the tetramer | Homo sapiens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-Serine + homocysteine | - |
Homo sapiens | Cystathionine + H2O | - |
? | |
| L-Serine + homocysteine | irreversible step in transsulfuration pathway | Homo sapiens | ? | - |
? | |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
dissociation of tetrameric enzyme to dimeric form, initiated by proteolysis decreases thermostability | Homo sapiens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| S-adenosyl-L-methionine | - |
Homo sapiens | |
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Release 2023.1 (January 2023)
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