Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.2.1.22 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
Search for more literature for 4.2.1.22

Activating Compound

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

Cloned(Commentary)

Cloned (Comment) Organism
-
 Homo sapiens

Protein Variants

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

Inhibitors

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
fibroblast
-
 Homo sapiens
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Temperature Stability [°C]

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

Cofactor

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