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Literature summary extracted from

  • Hilbi, H.; Dehning, I.; Schink, B.; Dimroth, P.
    Malonate decarboxylase of Malonomonas rubra, a novel type of biotin-containing acetyl enzyme (1992), Eur. J. Biochem., 207, 117-123.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.2.4.4 hydroxylamine complete inhibition Malonomonas rubra
7.2.4.4 thiocyanate complete inhibition Malonomonas rubra

Organism

EC Number Organism UniProt Comment Textmining
7.2.4.4 Malonomonas rubra
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
7.2.4.4 malonate + H+ + Na+[side 1] = acetate + CO2 + Na+[side 2] reaction does not involve intermediate formation of malonyl-CoA but proceeds directly with free malonate. Catalytic mechanism involves exchange of the enzyme-bound acetyl residues by malonyl residues and subsequent decarboxylation releasing CO2 and regenerating the acetyl-enzyme. Biotin is involved in catalysis Malonomonas rubra
a

Renatured (Commentary)

EC Number Renatured (Comment) Organism
7.2.4.4 enzyme inhibited by thiocyanate or hydroxylamine, 50-65% of the original decarboxylase activity is restored by incubation of the extract with ATP in the presence of acetate, and the extent of reactivation increases after incubation with dithioerythritol. Reactivation is also obtained by chemical acetylation with acetic anhydride Malonomonas rubra

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
7.2.4.4 2.67
-
 pH 7.5, 30°C Malonomonas rubra

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.2.4.4 malonate + H+
-
 Malonomonas rubra acetate + CO2
-
 ?