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Literature summary for 4.2.1.22 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
Search for more literature for 4.2.1.22

Cloned(Commentary)

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

Substrates and Products (Substrate)

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

Synonyms Comment Organism
CBS
-
 Homo sapiens

Cofactor

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