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Literature summary extracted from

  • Evande, R.; Blom, H.; Boers, G.H.; Banerjee, R.
    Alleviation of intrasteric inhibition by the pathogenic activation domain mutation, D444N, in human cystathionine beta-synthase (2002), Biochemistry, 41, 11832-11837.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.2.1.22 S-adenosyl-L-methionine 2fold activation, allosteric regulator Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.22
-
Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.22 D444N mutant is unresponsive to physiological S-adenosyl-L-methionine concentrations, but can be activated in the presence of supraphysiological concentrations Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.22 regulatory domain exerts an inhibitory effect on the enzyme, deletion is correlated with a 1fold increase in catalytic activity Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.22 Homo sapiens
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.2.1.22 fibroblast
-
Homo sapiens
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.2.1.22 2.65
-
wild-type enzyme in the presence of S-adenosyl-L-methionine Homo sapiens
4.2.1.22 3.95
-
D144N mutant in the presence of S-adenosyl-L-methionine Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.22 L-Serine + homocysteine
-
Homo sapiens Cystathionine + H2O
-
?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.2.1.22 48
-
stable up to Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
4.2.1.22 heme
-
Homo sapiens
4.2.1.22 pyridoxal 5'-phosphate
-
Homo sapiens