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 Commentary Textmining
Klebsiella pneumoniae
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Purification (Commentary)

Purification (Commentary) 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 Commentary Substrates Literature (Substrates) Organism Products Commentary (Products) Literature (Products) Organism (Products) Reversibility Substrate Product ID
additional information catalytic mechanism of malonate decarboxylase and involvement of ACP-SH acetate:ligase 686490 Klebsiella pneumoniae ?
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?

Purification (Commentary) (protein specific)

Commentary 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) (protein specific)

Substrates Commentary Substrates Literature (Substrates) Organism Products Commentary (Products) Literature (Products) Organism (Products) Reversibility ID
additional information catalytic mechanism of malonate decarboxylase and involvement of ACP-SH acetate:ligase 686490 Klebsiella pneumoniae ?
-
-
-
?