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Literature summary for 4.1.1.83 extracted from

  • Selvaraj, B.; Pierik, A.J.; Bill, E.; Martins, B.M.
    4-Hydroxyphenylacetate decarboxylase activating enzyme catalyses a classical S-adenosylmethionine reductive cleavage reaction (2013), J. Biol. Inorg. Chem., 18, 633-643.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Clostridium scatologenes

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
36000
-
x * 36000, SDS-PAGE Clostridium scatologenes

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-hydroxyphenylacetate + H+ Clostridium scatologenes
-
4-cresol + CO2
-
?

Organism

Organism UniProt Comment Textmining
Clostridium scatologenes
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-hydroxyphenylacetate + H+
-
Clostridium scatologenes 4-cresol + CO2
-
?

Subunits

Subunits Comment Organism
? x * 36000, SDS-PAGE Clostridium scatologenes

Synonyms

Synonyms Comment Organism
4Hpad
-
Clostridium scatologenes

Cofactor

Cofactor Comment Organism Structure
[4Fe-4S]-center the enzyme binds a maximum of two [4Fe-4S]2+/+ clusters Clostridium scatologenes