BRENDA - Enzyme Database
show all sequences of 2.1.3.10

Purification and characterization of a cytoplasmic enzyme component of the Na+-activated malonate decarboxylase system of Malonomonas rubra: acetyl-S-acyl carrier protein: malonate acyl carrier protein-SH transferase

Hilbi, H.; Dimroth, P.; Arch. Microbiol. 162, 48-56 (1994)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
citrate
-
Malonomonas rubra
malonate
-
Malonomonas rubra
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.5
-
malonate
pH 6.0
Malonomonas rubra
1.9
-
malonyl-CoA
pH 6.0
Malonomonas rubra
6.9
-
acetyl-CoA
pH 6.0
Malonomonas rubra
54
-
acetate
pH 6.0
Malonomonas rubra
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
59000
-
gel filtration
Malonomonas rubra
67000
-
1 * 67000, SDS-PAGE
Malonomonas rubra
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
acetyl-CoA + dephospho-CoA
Malonomonas rubra
-
CoA + acetyl-dephospho-CoA
-
-
r
malonyl-CoA + dephospho-CoA
Malonomonas rubra
-
CoA + malonyl-dephospho-CoA
-
-
r
additional information
Malonomonas rubra
enzyme catalyzes the transfer of acyl carrier protein from acetyl acyl carrier protein and malonate to yield malonyl acyl carrier protein and acetate. Malonate is thus activated on the enzyme by exchange for the catalytically important enzyme-bound acetyl thioester residues
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Malonomonas rubra
-
enzyme is part of the Na+-activied malonate decarboxylase system
-
Purification (Commentary)
Commentary
Organism
purification of subunit acetyl-S-acyl carrier protein: malonate acyl carrier protein-SH transferase
Malonomonas rubra
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
367
-
-
Malonomonas rubra
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
acetyl-CoA + dephospho-CoA
-
684745
Malonomonas rubra
CoA + acetyl-dephospho-CoA
-
-
-
r
malonyl-CoA + dephospho-CoA
-
684745
Malonomonas rubra
CoA + malonyl-dephospho-CoA
-
-
-
r
additional information
enzyme catalyzes the transfer of acyl carrier protein from acetyl acyl carrier protein and malonate to yield malonyl acyl carrier protein and acetate. Malonate is thus activated on the enzyme by exchange for the catalytically important enzyme-bound acetyl thioester residues
684745
Malonomonas rubra
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
monomer
1 * 67000, SDS-PAGE
Malonomonas rubra
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5.5
-
-
Malonomonas rubra
pH Range
pH Minimum
pH Maximum
Commentary
Organism
4.5
-
sharp decrease in activity from pH 5.5 to pH 4.5
Malonomonas rubra
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.4
-
malonate
pH 6.0
Malonomonas rubra
3
-
citrate
pH 6.0
Malonomonas rubra
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
citrate
-
Malonomonas rubra
malonate
-
Malonomonas rubra
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.4
-
malonate
pH 6.0
Malonomonas rubra
3
-
citrate
pH 6.0
Malonomonas rubra
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.5
-
malonate
pH 6.0
Malonomonas rubra
1.9
-
malonyl-CoA
pH 6.0
Malonomonas rubra
6.9
-
acetyl-CoA
pH 6.0
Malonomonas rubra
54
-
acetate
pH 6.0
Malonomonas rubra
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
59000
-
gel filtration
Malonomonas rubra
67000
-
1 * 67000, SDS-PAGE
Malonomonas rubra
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
acetyl-CoA + dephospho-CoA
Malonomonas rubra
-
CoA + acetyl-dephospho-CoA
-
-
r
malonyl-CoA + dephospho-CoA
Malonomonas rubra
-
CoA + malonyl-dephospho-CoA
-
-
r
additional information
Malonomonas rubra
enzyme catalyzes the transfer of acyl carrier protein from acetyl acyl carrier protein and malonate to yield malonyl acyl carrier protein and acetate. Malonate is thus activated on the enzyme by exchange for the catalytically important enzyme-bound acetyl thioester residues
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
purification of subunit acetyl-S-acyl carrier protein: malonate acyl carrier protein-SH transferase
Malonomonas rubra
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
367
-
-
Malonomonas rubra
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
acetyl-CoA + dephospho-CoA
-
684745
Malonomonas rubra
CoA + acetyl-dephospho-CoA
-
-
-
r
malonyl-CoA + dephospho-CoA
-
684745
Malonomonas rubra
CoA + malonyl-dephospho-CoA
-
-
-
r
additional information
enzyme catalyzes the transfer of acyl carrier protein from acetyl acyl carrier protein and malonate to yield malonyl acyl carrier protein and acetate. Malonate is thus activated on the enzyme by exchange for the catalytically important enzyme-bound acetyl thioester residues
684745
Malonomonas rubra
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 67000, SDS-PAGE
Malonomonas rubra
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5.5
-
-
Malonomonas rubra
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
4.5
-
sharp decrease in activity from pH 5.5 to pH 4.5
Malonomonas rubra
Other publictions for EC 2.1.3.10
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)
684745
Hilbi
Purification and characterizat ...
Malonomonas rubra
Arch. Microbiol.
162
48-56
1994
-
-
-
-
-
-
2
4
-
-
2
3
-
1
-
-
1
-
-
-
1
-
3
1
-
-
-
-
1
1
-
-
2
-
-
-
-
-
-
-
-
-
-
2
2
4
-
-
2
3
-
-
-
1
-
-
1
-
3
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-