BRENDA - Enzyme Database
show all sequences of 7.2.4.4

Malonate decarboxylase of Malonomonas rubra, a novel type of biotin-containing acetyl enzyme

Hilbi, H.; Dehning, I.; Schink, B.; Dimroth, P.; Eur. J. Biochem. 207, 117-123 (1992)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
hydroxylamine
complete inhibition
Malonomonas rubra
thiocyanate
complete inhibition
Malonomonas rubra
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Malonomonas rubra
-
-
-
Reaction
Reaction
Commentary
Organism
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
Renatured (Commentary)
Commentary
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]
Commentary
Organism
2.67
-
pH 7.5, 30°C
Malonomonas rubra
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
malonate + H+
-
686488
Malonomonas rubra
acetate + CO2
-
-
-
?
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
hydroxylamine
complete inhibition
Malonomonas rubra
thiocyanate
complete inhibition
Malonomonas rubra
Renatured (Commentary) (protein specific)
Commentary
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] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
2.67
-
pH 7.5, 30°C
Malonomonas rubra
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
malonate + H+
-
686488
Malonomonas rubra
acetate + CO2
-
-
-
?
Other publictions for EC 7.2.4.4
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
684746
Berg
The biotin protein MadF of the ...
Malonomonas rubra
Arch. Microbiol.
170
464-468
1998
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1
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1
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1
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1
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1
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-
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-
686491
Berg
Sequence of a gene cluster fro ...
Malonomonas rubra
Eur. J. Biochem.
245
103-115
1997
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1
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1
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1
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-
685053
Berg
The acyl carrier protein of ma ...
Malonomonas rubra
Biochemistry
35
4689-4696
1996
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1
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1
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1
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687270
Micklefield
-
Stereochemical course of malon ...
Malonomonas rubra
J. Am. Chem. Soc.
117
1153-1154
1995
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1
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1
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684745
Hilbi
Purification and characterizat ...
Malonomonas rubra
Arch. Microbiol.
162
48-56
1994
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1
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1
1
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2
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1
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1
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2
1
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1
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1
1
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1
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2
1
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684744
Hilbi
The malonate decarboxylase enz ...
Malonomonas rubra, Propionigenium modestum
Arch. Microbiol.
160
126-131
1993
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1
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4
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2
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1
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1
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2
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2
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1
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4
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1
1
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686488
Hilbi
Malonate decarboxylase of Malo ...
Malonomonas rubra
Eur. J. Biochem.
207
117-123
1992
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2
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1
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1
1
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1
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1
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