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Literature summary for 7.2.4.4 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
Search for more literature for 7.2.4.4

Inhibitors

Inhibitors Comment Organism Structure
hydroxylamine complete inhibition Malonomonas rubra
thiocyanate complete inhibition Malonomonas rubra

Organism

Organism UniProt Comment Textmining
Malonomonas rubra
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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)

Renatured (Comment) Organism
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]

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

Substrates and Products (Substrate)

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