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Literature summary for 4.2.1.22 extracted from

  • Taoka, S.; Ohja, S.; Shan, X.; Kruger, W.D.; Banerjee, R.
    Evidence for heme-mediated redox regulation of human cystathionine beta-synthase activity (1998), J. Biol. Chem., 273, 25179-25184.
    View publication on PubMed
Search for more literature for 4.2.1.22

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2
-
 L-Ser no influence of S-adenosyl-L-methionine, recombinant enzyme Homo sapiens
4.8
-
 homocysteine absence of S-adenosyl-L-methionine, recombinant enzyme Homo sapiens
5
-
 homocysteine presence of S-adenosyl-L-methionine, recombinant enzyme Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-Serine + homocysteine Homo sapiens
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.6
-
 recombinant enzyme 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
-
 Homo sapiens ?
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
 recombinant enzyme Homo sapiens

Cofactor

Cofactor Comment Organism Structure
heme 2 mol per mol of tetrameric enzyme Homo sapiens
pyridoxal 5'-phosphate 2 mol per mol of tetrameric enzyme Homo sapiens