BRENDA - Enzyme Database show

Purification and properties of bovine and human holocarboxylase synthetase

Suzuki, Y.; Narisawa, K.; Methods Enzymol. 279, 386-393 (1997)

Data extracted from this reference:

Application
EC Number
Application
Commentary
Organism
6.3.4.10
diagnostics
the HCS assay using rat liver apopropionyl-CoA carboxylase as substrate is useful for enzymatic diagnosis of HCS deficiency
Bos taurus
6.3.4.10
diagnostics
the HCS assay using rat liver apopropionyl-CoA carboxylase as substrate is useful for enzymatic diagnosis of HCS deficiency
Homo sapiens
Cloned(Commentary)
EC Number
Commentary
Organism
6.3.4.10
-
Homo sapiens
General Stability
EC Number
General Stability
Organism
6.3.4.10
after separation of the 64 kDa protein from an inert protein of 34 kDa on a nondenaturing PAGE, HCS is extremely labile and its enzymatic activity is totally lost within a few hours
Bos taurus
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
6.3.4.10
0.000013
-
biotin
; pH 8, 30°C, cosubstrate apo-PCC from biotin-deficient rat liver
Bos taurus
6.3.4.10
0.000013
-
biotin
-
Oryctolagus cuniculus
6.3.4.10
20
-
ATP
pH 8, 30°C, cosubstrate apo-PCC from biotin-deficient rat liver
Bos taurus
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
6.3.4.10
cytosol
-
Bos taurus
5829
-
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
6.3.4.10
64000
-
gel filtration, HCS seems to be partially degraded, the molecular mass may be 81-85 kDa, the 64 kDa protein purified through gel filtration is clearly separated from an inert protein of 34 kDa on a nondenaturing PAGE at pH 9.5 or 8
Bos taurus
6.3.4.10
80759
-
1 * 80759, amino acid sequence calculation; x * 80759, calculation from nucleotide sequence
Homo sapiens
6.3.4.10
81000
85000
-
Homo sapiens
6.3.4.10
81000
85000
-
Oryctolagus cuniculus
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
6.3.4.10
Bos taurus
-
-
-
6.3.4.10
Homo sapiens
-
-
-
6.3.4.10
Oryctolagus cuniculus
-
-
-
6.3.4.10
Rattus norvegicus
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
6.3.4.10
-
Homo sapiens
6.3.4.10
-
Bos taurus
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
6.3.4.10
liver
-
Bos taurus
-
6.3.4.10
liver
-
Oryctolagus cuniculus
-
6.3.4.10
liver
-
Rattus norvegicus
-
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
6.3.4.10
additional information
-
-
Bos taurus
6.3.4.10
additional information
-
-
Oryctolagus cuniculus
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6.3.4.10
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1390
Homo sapiens
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1390
Homo sapiens
-
6.3.4.10
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1390
Rattus norvegicus
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1390
Rattus norvegicus
-
6.3.4.10
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1390
Bos taurus
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1390
Bos taurus
-
6.3.4.10
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1390
Oryctolagus cuniculus
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1390
Oryctolagus cuniculus
-
6.3.4.10
ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
HCS catalyzes the incorporation of biotin into carboxylases, holo-PCC is formed from the apo-PCC
1390
Homo sapiens
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
6.3.4.10
ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
HCS catalyzes the incorporation of biotin into carboxylases, holo-PCC is formed from the apo-PCC from biotin-deficient rat liver or human lymphoblast in the presence of d-biotin and ATP, much higher activity with apo-PCC from rat livers than from human lymphoblasts
1390
Bos taurus
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
6.3.4.10
ATP + biotin + apocarboxyl carrier protein
HCS catalyzes the incorporation of biotin into carboxylases, recombinant apo-CCP from Escherichia coli
1390
Bos taurus
AMP + diphosphate + holocarboxyl carrier protein
-
-
-
?
6.3.4.10
CTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1390
Oryctolagus cuniculus
CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
6.3.4.10
CTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
as active as ATP
1390
Bos taurus
CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
6.3.4.10
CTP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
CTP can totally replace ATP
1390
Bos taurus
CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
6.3.4.10
GTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1390
Oryctolagus cuniculus
GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
6.3.4.10
GTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
50% of the activity relative to ATP
1390
Bos taurus
GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
6.3.4.10
GTP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
GTP is approximately half as active as ATP
1390
Bos taurus
GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
6.3.4.10
ITP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
50% of the activity relative to ATP
1390
Bos taurus
IMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
6.3.4.10
ITP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
ITP is approximately half as active as ATP
1390
Bos taurus
IMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
6.3.4.10
?
x * 80759, calculation from nucleotide sequence
Homo sapiens
6.3.4.10
monomer
1 * 80759, amino acid sequence calculation
Homo sapiens
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
6.3.4.10
30
-
assay at
Bos taurus
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.3.4.10
8
-
assay at
Bos taurus
Application (protein specific)
EC Number
Application
Commentary
Organism
6.3.4.10
diagnostics
the HCS assay using rat liver apopropionyl-CoA carboxylase as substrate is useful for enzymatic diagnosis of HCS deficiency
Bos taurus
6.3.4.10
diagnostics
the HCS assay using rat liver apopropionyl-CoA carboxylase as substrate is useful for enzymatic diagnosis of HCS deficiency
Homo sapiens
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
6.3.4.10
-
Homo sapiens
General Stability (protein specific)
EC Number
General Stability
Organism
6.3.4.10
after separation of the 64 kDa protein from an inert protein of 34 kDa on a nondenaturing PAGE, HCS is extremely labile and its enzymatic activity is totally lost within a few hours
Bos taurus
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
6.3.4.10
0.000013
-
biotin
; pH 8, 30°C, cosubstrate apo-PCC from biotin-deficient rat liver
Bos taurus
6.3.4.10
0.000013
-
biotin
-
Oryctolagus cuniculus
6.3.4.10
20
-
ATP
pH 8, 30°C, cosubstrate apo-PCC from biotin-deficient rat liver
Bos taurus
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
6.3.4.10
cytosol
-
Bos taurus
5829
-
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
6.3.4.10
64000
-
gel filtration, HCS seems to be partially degraded, the molecular mass may be 81-85 kDa, the 64 kDa protein purified through gel filtration is clearly separated from an inert protein of 34 kDa on a nondenaturing PAGE at pH 9.5 or 8
Bos taurus
6.3.4.10
80759
-
1 * 80759, amino acid sequence calculation; x * 80759, calculation from nucleotide sequence
Homo sapiens
6.3.4.10
81000
85000
-
Homo sapiens
6.3.4.10
81000
85000
-
Oryctolagus cuniculus
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
6.3.4.10
-
Homo sapiens
6.3.4.10
-
Bos taurus
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
6.3.4.10
liver
-
Bos taurus
-
6.3.4.10
liver
-
Oryctolagus cuniculus
-
6.3.4.10
liver
-
Rattus norvegicus
-
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
6.3.4.10
additional information
-
-
Bos taurus
6.3.4.10
additional information
-
-
Oryctolagus cuniculus
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
6.3.4.10
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1390
Homo sapiens
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1390
Homo sapiens
-
6.3.4.10
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1390
Rattus norvegicus
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1390
Rattus norvegicus
-
6.3.4.10
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1390
Bos taurus
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1390
Bos taurus
-
6.3.4.10
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1390
Oryctolagus cuniculus
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1390
Oryctolagus cuniculus
-
6.3.4.10
ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
HCS catalyzes the incorporation of biotin into carboxylases, holo-PCC is formed from the apo-PCC
1390
Homo sapiens
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
6.3.4.10
ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
HCS catalyzes the incorporation of biotin into carboxylases, holo-PCC is formed from the apo-PCC from biotin-deficient rat liver or human lymphoblast in the presence of d-biotin and ATP, much higher activity with apo-PCC from rat livers than from human lymphoblasts
1390
Bos taurus
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
6.3.4.10
ATP + biotin + apocarboxyl carrier protein
HCS catalyzes the incorporation of biotin into carboxylases, recombinant apo-CCP from Escherichia coli
1390
Bos taurus
AMP + diphosphate + holocarboxyl carrier protein
-
-
-
?
6.3.4.10
CTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1390
Oryctolagus cuniculus
CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
6.3.4.10
CTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
as active as ATP
1390
Bos taurus
CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
6.3.4.10
CTP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
CTP can totally replace ATP
1390
Bos taurus
CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
6.3.4.10
GTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1390
Oryctolagus cuniculus
GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
6.3.4.10
GTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
50% of the activity relative to ATP
1390
Bos taurus
GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
6.3.4.10
GTP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
GTP is approximately half as active as ATP
1390
Bos taurus
GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
6.3.4.10
ITP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
50% of the activity relative to ATP
1390
Bos taurus
IMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
6.3.4.10
ITP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
ITP is approximately half as active as ATP
1390
Bos taurus
IMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
6.3.4.10
?
x * 80759, calculation from nucleotide sequence
Homo sapiens
6.3.4.10
monomer
1 * 80759, amino acid sequence calculation
Homo sapiens
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
6.3.4.10
30
-
assay at
Bos taurus
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.3.4.10
8
-
assay at
Bos taurus