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Literature summary extracted from

  • Carballal, S.; Madzelan, P.; Zinola, C.F.; Grana, M.; Radi, R.; Banerjee, R.; Alvarez, B.
    Dioxygen reactivity and heme redox potential of truncated human cystathionine beta-synthase (2008), Biochemistry, 47, 3194-3201.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.22 in a recombinant expression system (pGEX4T1/hCBSDELTAC143) that produces a fusion protein with glutathione S-transferase Homo sapiens

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 Homo sapiens the oxidation of CBS by dioxygen appears to proceed directly from the ferrous to the ferric state, presumably via an outer sphere electron transfer reaction ?
-
 ?

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.22
-
 Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.22 L-serine + L-homocysteine
-
 Homo sapiens L-cystathionine + H2O
-
 ?
4.2.1.22 additional information the oxidation of CBS by dioxygen appears to proceed directly from the ferrous to the ferric state, presumably via an outer sphere electron transfer reaction Homo sapiens ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.2.1.22 CBS
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
4.2.1.22 heme heme in CBS is six-coordinate, low spin, and contains cysteine and histidine as axial ligands, the unusual heme in CBS represents a potential source of cytosolic superoxide radical Homo sapiens
4.2.1.22 pyridoxal 5'-phosphate
-
 Homo sapiens