Information on EC 6.3.4.10 - biotin-[propionyl-CoA-carboxylase (ATP-hydrolysing)] ligase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
6.3.4.10
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RECOMMENDED NAME
GeneOntology No.
biotin-[propionyl-CoA-carboxylase (ATP-hydrolysing)] ligase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amination
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biotin metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
biotin:apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)] ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
37318-67-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
2 enzyme forms: the major form is specific for the cytosol compartment, whereas the minor form is present in mitochondria as well as in chloroplasts
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + biotin + apo-beta-methylcrotonyl-CoA carboxylase
AMP + diphosphate + holo-beta-methylcrotonyl-CoA carboxylase
show the reaction diagram
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-
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?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
?
show the reaction diagram
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
show the reaction diagram
ATP + biotin + apo-[propionyl CoA carboxylase]
AMP + diphosphate + propionyl CoA carboxylase
show the reaction diagram
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?
ATP + biotin + apo-[propionyl-CoA carboxylase]
AMP + diphosphate + propionyl-CoA carboxylase
show the reaction diagram
ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
show the reaction diagram
ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
show the reaction diagram
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-
-
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?
ATP + biotin + apoacetyl-CoA carboxylase
AMP + diphosphate + holoacetyl-CoA carboxylase
show the reaction diagram
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biotinylation of cytosolic ACC
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?
ATP + biotin + apocarboxyl carrier protein
AMP + diphosphate + holocarboxyl carrier protein
show the reaction diagram
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HCS catalyzes the incorporation of biotin into carboxylases, recombinant apo-CCP from Escherichia coli
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?
ATP + biotin + apocarboxylase
AMP + diphosphate + holocarboxylase
show the reaction diagram
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?
ATP + biotin + apopropionyl-CoA carboxylase
AMP + diphosphate + holopropionyl-CoA carboxylase
show the reaction diagram
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biotinylation of mitochondrial PCC
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?
ATP + biotin + apopyruvate carboxylase
AMP + diphosphate + holopyruvate carboxylase
show the reaction diagram
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?
ATP + biotin + BCCP87
AMP + diphosphate + biotin-BCCP87
show the reaction diagram
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substrate is the biotinoyl domain, BCCP87, of Escherichia coli biotin carboxyl carrier protein, BCCP, binding pattern, overview
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?
ATP + biotin + histone H2A
AMP + diphosphate + biotin-histone H2A
show the reaction diagram
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pattern of biotin attachment and comparison to nonenzymatic biotinylation of histone H2A, none of the lysine sites within histone H2A resembles the biotin attachment consensus sequence seen in carboxylases, mechanism, overview. H2A is a poor substrate for biotin attachment compared to the apocarboxylase biotin-attachment domain
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?
ATP + biotin + histone H3.2
AMP + diphosphate + biotin-histone H3.2
show the reaction diagram
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biotinylation of residues K9 and K18 in histone H3
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?
ATP + biotin + histone H3.2 N-terminal amino acids 1-25
AMP + diphosphate + biotin-histone H3.2 N-terminal amino acids 1-25
show the reaction diagram
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biotinylation of residues K9 and K18
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?
ATP + biotin + histone H4
AMP + diphosphate + biotin-histone H4
show the reaction diagram
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biotinylation at Lys12 especially in telomeric repeats, overview
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?
ATP + biotin + p67
AMP + diphosphate + biotinyl-p67
show the reaction diagram
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comprises the 67 C-terminal amino acids in human propionyl-CoA carboxylase, including the biotin-binding site lysine-669
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?
ATP + biotin + protein Syn67
AMP + diphosphate + protein Syn67-biotin
show the reaction diagram
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mutated Syn67, both N- and C-termini of HCS interact with Syn67, a polypeptide with a basic patch of lysines and arginines, and the Syn67 docking site is located near the active pocket of HCS. The target lysine in Syn67 is biotinylated by HCS only after arginine-to-glycine substitutions in Syn67 produce a histone-like peptide, binding structure, modelling, overview
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?
CTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
show the reaction diagram
CTP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
show the reaction diagram
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CTP can totally replace ATP
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?
GTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
show the reaction diagram
GTP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
show the reaction diagram
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GTP is approximately half as active as ATP
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?
ITP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
IMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
show the reaction diagram
ITP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
IMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
show the reaction diagram
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ITP is approximately half as active as ATP
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?
UTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
UMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
?
show the reaction diagram
ATP + biotin + apo-[propionyl CoA carboxylase]
AMP + diphosphate + propionyl CoA carboxylase
show the reaction diagram
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?
ATP + biotin + apo-[propionyl-CoA carboxylase]
AMP + diphosphate + propionyl-CoA carboxylase
show the reaction diagram
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?
ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
show the reaction diagram
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?
ATP + biotin + apocarboxylase
AMP + diphosphate + holocarboxylase
show the reaction diagram
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?
ATP + biotin + histone H4
AMP + diphosphate + biotin-histone H4
show the reaction diagram
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biotinylation at Lys12 especially in telomeric repeats, overview
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
p-Chloromercuriphenylsulfonate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000385 - 20
ATP
0.0000047 - 0.0033
biotin
0.0056
biotinyl-AMP
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4.1
p67
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pH 8.0, 37°C
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additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.514
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additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41172
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x * 41172, calculation from nucleotide sequence
60000
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gel filtration
80759
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1 * 80759, amino acid sequence calculation; x * 80759, calculation from nucleotide sequence
81000 - 85000
81000
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full-length HCS
115000
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N-terminal glutathione S transferase-tagged enzyme, x * 115000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53
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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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
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loss of activity upon freezing
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, 0.5 M sucrose, stable for about 1 week
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4°C, stable for several weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
apocarboxylase
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recombinant His-tagged HCS isozymes from Escherichia coli strain Rosetta(DE3)
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in HEK-293 cells
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expression in Escherichia coli
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expression of HCS and HCS-green fluorescent protein fusion protein in HEK-293 cells
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expression of p67 and truncated HCS in Saccharomyces cerevisiae for interaction analysis in the two-hybrid system, overview. Usage of derivatives of Saccharomyces cerevisiae wild-type strain W303
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expression of the two His-tagged HCS isozymes in Escherichia coli strain Rosetta(DE3)
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fusion of full-length HCS to DNA adenine methyltransferase Dam and subsequent transfection into breast cancer cells MCF-7 and normal breast cells MCF-10A
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HCS fused to glutathione S-transferase, S-tag, and both N-terminal and C-terminal 6x His-tags
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HLCS is encoded by an 11-exon gene, HLCS, located on chromosome 21q22.1, genotyping
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transgenic HEK-293 cells that overexpress HCS fused to green fluorescent protein
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
evolutionary conserved binding site for microRNA miR-539 in the 3'-untranslated region of HCS mRNA. miR-539 decreases the expression of HCS at the level of transcription rather than translation. When miR-539 is overexpressed in transgenic cells, the abundance of both HCS and biotinylated histones decreases. The abundance of miR-539 is tissue dependent, decreasing in the order fibroblasts, kidney cells, intestinal cells, lymphoid cells. The abundance of miR-539 is significantly higher at physiological concentrations of biotin than both biotin-deficient and biotin-supplemented media in all cell lines tested
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D571N
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mutation within the biotin-binding region, HCS deficiency, biotin-responsive multiple carboxylase deficiency
G518E
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mutation within the biotin-binding region, HCS deficiency, biotin-responsive multiple carboxylase deficiency
L216R
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mutation outside the biotin-binding region, HCS deficiency, biotin-responsive multiple carboxylase deficiency
R508W
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mutation within the biotin-binding region, HCS deficiency, biotin-responsive multiple carboxylase deficiency
V363D
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mutation outside the biotin-binding region, HCS deficiency, biotin-responsive multiple carboxylase deficiency
V550M
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mutation within the biotin-binding region, HCS deficiency, biotin-responsive multiple carboxylase deficiency
additional information
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identification of naturally occuring mutations leading to multiple carboxylase deficiency, MCD, an autosomal recessive metabolic disorder caused by HLCS deficiency, overview
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
diagnostics
medicine
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HCS deficiency results in biotin-responsive multiple carboxylase deficiency