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Literature summary for 6.2.1.35 extracted from

  • Schmid, M.; Berg, M.; Hilbi, H.; Dimroth, P.
    Malonate decarboxylase of Klebsiella pneumoniae catalyses the turnover of acetyl and malonyl thioester residues on a coenzyme-A-like prosthetic group (1996), Eur. J. Biochem., 237, 221-228.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Klebsiella pneumoniae
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Purification (Commentary)

Purification (Comment) Organism
during purification of the malonate decarboxylase complex, the ligase is separated from the decarboxylase by treatment with 1.5 M ammonium sulfate after the TSK-DEAE column Klebsiella pneumoniae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information catalytic mechanism of malonate decarboxylase and involvement of ACP-SH acetate:ligase Klebsiella pneumoniae ?
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