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Literature summary extracted from

  • Banerjee, R.; Evande, R.; Kabil, O.; Ojha, S.; Taoka, S.
    Reaction mechanism and regulation of cystathionine beta-synthase (2003), Biochim. Biophys. Acta, 1647, 30-35.
    View publication on PubMed

Activating Compound

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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.22
-
Homo sapiens
4.2.1.22
-
Saccharomyces cerevisiae

Protein Variants

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

Inhibitors

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

Natural Substrates/ Products (Substrates)

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 ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.22 Homo sapiens
-
-
-
4.2.1.22 Mammalia
-
-
-
4.2.1.22 Saccharomyces cerevisiae
-
-
-

Reaction

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

Source Tissue

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

Substrates and Products (Substrate)

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 ?
-
?

Subunits

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

Cofactor

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