BRENDA - Enzyme Database
show all sequences of 6.3.4.10

The enzymatic synthesis of propionyl coenzyme A holocarboxylase from d-biotinyl 5'-adenylate and the apocarboxylase

Siegel, L.; Foote, J.L.; Coon, M.J.; J. Biol. Chem. 240, 1025-1031 (1965)

Data extracted from this reference:

General Stability
General Stability
Organism
loss of activity upon freezing
Oryctolagus cuniculus
Inhibitors
Inhibitors
Commentary
Organism
Structure
p-chloromercuriphenylsulfonate
-
Oryctolagus cuniculus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0000047
-
biotin
-
Oryctolagus cuniculus
0.000385
-
ATP
-
Oryctolagus cuniculus
0.0013
-
ATP
-
Oryctolagus cuniculus
0.0056
-
biotinyl-AMP
-
Oryctolagus cuniculus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
Mg2+ is probably required primarily for the synthesis of biotinyl-AMP from ATP and biotin, but not for the transfer of the biotin moiety from this intermediate to the apocarboxylase; required
Oryctolagus cuniculus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
Oryctolagus cuniculus
-
?
-
-
-
Organism
Organism
UniProt
Commentary
Textmining
Oryctolagus cuniculus
-
-
-
Rattus norvegicus
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
-
Oryctolagus cuniculus
apocarboxylase
Rattus norvegicus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
liver
-
Rattus norvegicus
-
liver
-
Oryctolagus cuniculus
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Oryctolagus cuniculus
Storage Stability
Storage Stability
Organism
0°C, 0.5 M sucrose, stable for about 1 week
Oryctolagus cuniculus
4°C, stable for several weeks
Oryctolagus cuniculus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1394
Rattus norvegicus
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1394
Rattus norvegicus
-
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
biotinyl-AMP is an intermediate
1394
Oryctolagus cuniculus
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1394
Oryctolagus cuniculus
-
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1394
Oryctolagus cuniculus
?
-
-
-
-
CTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
19% of the activity relative to ATP
1394
Oryctolagus cuniculus
CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
GTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
11% of the activity relative to ATP
1394
Oryctolagus cuniculus
GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
UTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
24% of the activity relative to ATP
1394
Oryctolagus cuniculus
UMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
53
-
10-19% loss of activity after 1 min, 73-76% loss of activity after 5 min, 91-93% loss of activity after 15 min; 10% loss of activity after 1 min, 63% loss of activity after 5 min, 91% loss of activity after 15 min
Oryctolagus cuniculus
General Stability (protein specific)
General Stability
Organism
loss of activity upon freezing
Oryctolagus cuniculus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
p-chloromercuriphenylsulfonate
-
Oryctolagus cuniculus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0000047
-
biotin
-
Oryctolagus cuniculus
0.000385
-
ATP
-
Oryctolagus cuniculus
0.0013
-
ATP
-
Oryctolagus cuniculus
0.0056
-
biotinyl-AMP
-
Oryctolagus cuniculus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
Mg2+ is probably required primarily for the synthesis of biotinyl-AMP from ATP and biotin, but not for the transfer of the biotin moiety from this intermediate to the apocarboxylase; required
Oryctolagus cuniculus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
Oryctolagus cuniculus
-
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
-
Oryctolagus cuniculus
apocarboxylase
Rattus norvegicus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
liver
-
Rattus norvegicus
-
liver
-
Oryctolagus cuniculus
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Oryctolagus cuniculus
Storage Stability (protein specific)
Storage Stability
Organism
0°C, 0.5 M sucrose, stable for about 1 week
Oryctolagus cuniculus
4°C, stable for several weeks
Oryctolagus cuniculus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1394
Rattus norvegicus
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1394
Rattus norvegicus
-
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
biotinyl-AMP is an intermediate
1394
Oryctolagus cuniculus
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1394
Oryctolagus cuniculus
-
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
1394
Oryctolagus cuniculus
?
-
-
-
-
CTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
19% of the activity relative to ATP
1394
Oryctolagus cuniculus
CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
GTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
11% of the activity relative to ATP
1394
Oryctolagus cuniculus
GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
UTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
24% of the activity relative to ATP
1394
Oryctolagus cuniculus
UMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
53
-
10-19% loss of activity after 1 min, 73-76% loss of activity after 5 min, 91-93% loss of activity after 15 min; 10% loss of activity after 1 min, 63% loss of activity after 5 min, 91% loss of activity after 15 min
Oryctolagus cuniculus
Other publictions for EC 6.3.4.10
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
Synonyms
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)
745784
Donti
Holocarboxylase synthetase de ...
Homo sapiens
Mol. Genet. Metab. Rep.
7
40-44
2016
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1
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4
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-
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3
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1
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4
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-
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-
-
-
-
744011
Miyao
Immobilization of immunoglobu ...
Sulfurisphaera tokodaii, Sulfurisphaera tokodaii DSM 16993
Anal. Biochem.
484
113-121
2015
-
1
-
-
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-
-
5
-
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1
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1
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-
726655
Xue
Holocarboxylase synthetase cat ...
Homo sapiens
Am. J. Physiol. Cell Physiol.
305
C1240-C1245
2013
-
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1
1
-
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728180
Li
Holocarboxylase synthetase int ...
Homo sapiens
J. Nutr. Biochem.
24
1446-1452
2013
-
-
-
-
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1
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1
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1
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-
1
1
-
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-
713742
Singh
Identification of holocarboxyl ...
Homo sapiens
Anal. Biochem.
413
55-59
2011
-
1
1
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1
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2
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1
1
-
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714763
Rios-Avila
A 96-well plate assay for high ...
Homo sapiens
Clin. Chim. Acta
412
735-739
2011
-
1
1
-
-
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1
-
-
-
-
-
4
-
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1
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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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1
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715997
Bao
Holocarboxylase synthetase is ...
Homo sapiens
J. Nutr. Biochem.
22
470-475
2011
-
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1
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1
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4
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1
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3
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1
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1
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3
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1
1
-
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716237
Reyes-Carmona
Trafficking and chromatin dyna ...
Drosophila melanogaster
Mol. Genet. Metab.
103
240-248
2011
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1
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2
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2
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2
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2
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1
1
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726859
Bao
Human holocarboxylase syntheta ...
Homo sapiens
Biochem. Biophys. Res. Commun.
412
115-120
2011
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1
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2
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1
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1
1
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701935
Hassan
The polypeptide Syn67 interact ...
Homo sapiens
Arch. Biochem. Biophys.
495
35-41
2010
-
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1
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701936
Bailey
Holocarboxylase synthetase: co ...
Homo sapiens
Arch. Biochem. Biophys.
496
45-52
2010
-
-
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-
-
-
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5
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2
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1
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4
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4
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2
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2
2
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703738
Lee
The N-terminal domain of human ...
Homo sapiens
FEBS Lett.
584
675-680
2010
-
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1
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1
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3
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2
1
2
1
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1
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2
1
1
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1
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1
1
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705293
Wijeratne
K12-biotinylated histone H4 is ...
Homo sapiens
J. Nutr. Biochem.
21
310-316
2010
-
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2
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2
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2
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1
1
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715999
Bao
Biotin regulates the expressio ...
Homo sapiens
J. Nutr.
140
1546-1551
2010
-
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1
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4
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1
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1
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702499
Zempleni
Biotin ...
Homo sapiens
Biofactors
35
36-46
2009
-
-
-
-
-
-
-
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1
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2
-
2
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3
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2
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1
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1
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1
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2
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3
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2
2
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702952
Yokoi
A case of holocarboxylase synt ...
Homo sapiens
Brain Dev.
31
775-778
2009
-
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1
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1
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1
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1
1
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-
703282
Tammachote
Holocarboxylase synthetase def ...
Homo sapiens
Clin. Genet.
78
88-93
2009
-
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1
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1
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2
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