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Literature summary for 6.3.4.10 extracted from

  • Suzuki, Y.; Narisawa, K.
    Purification and properties of bovine and human holocarboxylase synthetase (1997), Methods Enzymol., 279, 386-393.
    View publication on PubMed

Application

Application Comment Organism
diagnostics the HCS assay using rat liver apopropionyl-CoA carboxylase as substrate is useful for enzymatic diagnosis of HCS deficiency Homo sapiens
diagnostics the HCS assay using rat liver apopropionyl-CoA carboxylase as substrate is useful for enzymatic diagnosis of HCS deficiency Bos taurus

Cloned(Commentary)

Cloned (Comment) Organism
-
Homo sapiens

General Stability

General Stability Organism
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.000013
-
biotin
-
Bos taurus
0.000013
-
biotin
-
Oryctolagus cuniculus
0.000013
-
biotin pH 8, 30°C, cosubstrate apo-PCC from biotin-deficient rat liver Bos taurus
20
-
ATP pH 8, 30°C, cosubstrate apo-PCC from biotin-deficient rat liver Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Bos taurus 5829
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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
80759
-
x * 80759, calculation from nucleotide sequence Homo sapiens
80759
-
1 * 80759, amino acid sequence calculation Homo sapiens
81000 85000
-
Homo sapiens
81000 85000
-
Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-
Homo sapiens
-
-
-
Oryctolagus cuniculus
-
-
-
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens
-
Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-
liver
-
Bos taurus
-
liver
-
Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Bos taurus
additional information
-
-
Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
Homo sapiens AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
Rattus norvegicus AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
Bos taurus AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
Oryctolagus cuniculus AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
?
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 Homo sapiens AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
?
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 Bos taurus AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
?
ATP + biotin + apocarboxyl carrier protein HCS catalyzes the incorporation of biotin into carboxylases, recombinant apo-CCP from Escherichia coli Bos taurus AMP + diphosphate + holocarboxyl carrier protein
-
?
CTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
Oryctolagus cuniculus CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
?
CTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)] as active as ATP Bos taurus CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
?
CTP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] CTP can totally replace ATP Bos taurus CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
?
GTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
Oryctolagus cuniculus GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
?
GTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)] 50% of the activity relative to ATP Bos taurus GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
?
GTP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] GTP is approximately half as active as ATP Bos taurus GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
?
ITP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)] 50% of the activity relative to ATP Bos taurus IMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
?
ITP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] ITP is approximately half as active as ATP Bos taurus IMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
?

Subunits

Subunits Comment Organism
? x * 80759, calculation from nucleotide sequence Homo sapiens
monomer 1 * 80759, amino acid sequence calculation Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Bos taurus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Bos taurus