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Information on EC 6.3.4.10 - biotin-[propionyl-CoA-carboxylase (ATP-hydrolysing)] ligase
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6.3.4.10 biotin-[propionyl-CoA-carboxylase (ATP-hydrolysing)] ligaseSpecify your search results
Word Map
- 6.3.4.10
-
biotinylation
- carboxylases
-
biotin-dependent
- histone
- biotinidase
- acidosis
-
biotin-responsive
-
multivitamin
- aciduria
-
biotinyl-5\'-amp
-
biotin-deficient
- apocarboxylases
-
methylcitrate
-
3-hydroxyisovaleric
-
hyperammonemia
- tokodaii
- 3-methylcrotonyl-coa
-
biotin-binding
- diagnostics
- medicine
- analysis
- synthesis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
holocarboxylase synthetase, biotin protein ligase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Biotin-propionyl coenzyme A carboxylase synthetase
-
-
-
-
Biotin-[propionyl-CoA-carboxylase (ATP-hydrolysing)] synthetase
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-
-
-
BPL
HCS
Holocarboxylase synthetase
Propionyl coenzyme A holocarboxylase synthetase
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-
-
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Synthetase, biotin-propionyl coenzyme A carboxylase
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-
-
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HCS
-
-
-
-
HCS
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-
Holocarboxylase synthetase
-
-
-
-
Holocarboxylase synthetase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amination
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-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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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
37318-67-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + biotin + apo-beta-methylcrotonyl-CoA carboxylase
AMP + diphosphate + holo-beta-methylcrotonyl-CoA carboxylase
-
-
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
ATP + biotin + apo-[propionyl CoA carboxylase]
AMP + diphosphate + propionyl CoA carboxylase
-
-
-
-
?
ATP + biotin + apo-[propionyl-CoA carboxylase]
AMP + diphosphate + propionyl-CoA carboxylase
ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + apoacetyl-CoA carboxylase
AMP + diphosphate + holoacetyl-CoA carboxylase
-
biotinylation of cytosolic ACC
-
-
?
ATP + biotin + apocarboxyl carrier protein
AMP + diphosphate + holocarboxyl carrier protein
-
HCS catalyzes the incorporation of biotin into carboxylases, recombinant apo-CCP from Escherichia coli
-
-
?
ATP + biotin + apopropionyl-CoA carboxylase
AMP + diphosphate + holopropionyl-CoA carboxylase
-
biotinylation of mitochondrial PCC
-
-
?
ATP + biotin + apopyruvate carboxylase
AMP + diphosphate + holopyruvate carboxylase
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-
-
-
?
ATP + biotin + BCCP87
AMP + diphosphate + biotin-BCCP87
-
substrate is the biotinoyl domain, BCCP87, of Escherichia coli biotin carboxyl carrier protein, BCCP, binding pattern, overview
-
-
?
ATP + biotin + histone H2A
AMP + diphosphate + biotin-histone H2A
-
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
-
-
?
ATP + biotin + histone H3.2
AMP + diphosphate + biotin-histone H3.2
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-
biotinylation of residues K9 and K18 in histone H3
-
?
ATP + biotin + histone H3.2 N-terminal amino acids 1-25
AMP + diphosphate + biotin-histone H3.2 N-terminal amino acids 1-25
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-
biotinylation of residues K9 and K18
-
?
ATP + biotin + histone H4
AMP + diphosphate + biotin-histone H4
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biotinylation at Lys12 especially in telomeric repeats, overview
-
-
?
ATP + biotin + p67
AMP + diphosphate + biotinyl-p67
-
comprises the 67 C-terminal amino acids in human propionyl-CoA carboxylase, including the biotin-binding site lysine-669
-
-
?
ATP + biotin + protein Syn67
AMP + diphosphate + protein Syn67-biotin
-
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)]
CTP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
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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)]
GTP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
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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)]
ITP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
IMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
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ITP is approximately half as active as ATP
-
-
?
UTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
UMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
?
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plays an essential role in biotin utilization
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?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
?
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its deficiency causes biotin-responsive multiple carboxylase deficiency in humans
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?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
?
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-
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
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-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
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biotinylates apopropionyl-CoA carboxylase from patients with holocarboxylase synthetase deficiency
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?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
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-
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?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
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-
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?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
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biotinyl-AMP is an intermediate
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?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
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the alpha-subunit of propionyl-CoA carboxylase and its mature counterpart are competent for biotinylation
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?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
?
ATP + biotin + apo-[propionyl-CoA carboxylase]
AMP + diphosphate + propionyl-CoA carboxylase
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-
-
-
?
ATP + biotin + apo-[propionyl-CoA carboxylase]
AMP + diphosphate + propionyl-CoA carboxylase
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substrate is p67, the carboxyl-terminal fragment of the propionyl-CoA-carboxylase alpha subunit, the substrate is biotinylated at Lys67
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-
?
ATP + biotin + apo-[propionyl-CoA carboxylase]
AMP + diphosphate + propionyl-CoA carboxylase
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substrate is p67, the carboxyl-terminal fragment of the propionyl-CoA-carboxylase alpha subunit, the substrate is biotinylated at Lys67. Determination of amino acid of HCS involved in the interaction, docking of p67 near Arg508 and Ser515 within the central domain of HCS, overview
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-
?
ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
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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
-
-
?
ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
HCS catalyzes the incorporation of biotin into carboxylases, holo-PCC is formed from the apo-PCC
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-
?
CTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
as active as ATP
-
-
?
CTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
117% of the activity relative to ATP
-
-
?
CTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
28% of the activity relative to ATP
-
-
?
CTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
CTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
CMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
19% of the activity relative to ATP
-
-
?
GTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
50% of the activity relative to ATP
-
-
?
GTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
46% of the activity relative to ATP
-
-
?
GTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
GTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
GTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
GMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
11% of the activity relative to ATP
-
-
?
ITP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
IMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
50% of the activity relative to ATP
-
-
?
ITP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
IMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
47% of the activity relative to ATP
-
-
?
ITP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
IMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
UTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
UMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
95% of the activity relative to ATP
-
-
?
UTP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
UMP + diphosphate + [propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
24% of the activity relative to ATP
-
-
?
additional information
?
-
-
HCS catalyzes the ATP-dependent biotinylation of the four biotin-dependent carboxylases found in humans
-
-
?
additional information
?
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although mammals have multiple biotin-dependent enzymes there is only a single gene encoding holocarboxylase synthetase, HCS, responsible for all cellular biotinylation. The enzyme catalyzes the reactions of EC 6.3.4.10, EC 6.3.4.11, and EC 6.3.4.15, overview
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-
?
additional information
?
-
-
holocarboxylase synthetase catalyzes the attachment of biotin to the epsilon-amino group of a specific lysine residue in apocarboxylases, biotinylation of biotin-dependent carboxylases requires ATP and proceeds in the following two steps
-
-
?
additional information
?
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holocarboxylase synthetase, HCS, catalyzes the binding of biotin to lysines in carboxylases and histones in two steps. First, HCS catalyzes the synthesis of biotinyl-5'-AMP, and second, the biotinyl moiety is ligated to lysine residues, binding structure, modelling, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the reactions of EC 6.3.4.10, EC 6.3.4.11, and EC 6.3.4.15, overview
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-
?
additional information
?
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the 4'-hydroxyazobenzene-2-carboxylic acid dye assay can be used to quantify biotin
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?
additional information
?
-
-
the N-terminal domain of hHCS recognizes the charged region of biotin acceptor protein, distinctly from the recognition by the catalytic domain
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-
?
additional information
?
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-
the enzyme is critical to utilization of exogenous or dietary biotin and responds to biotin deprivation by reduction in the steady state level of their mRNAs. The free biotin is directed to brain because the reduction in holocarboxylase synthetase, sodium-dependent multivitamin-transporter and carboxylase mRNAs in liver reduces their capacity to utilize biotin while leaving free biotin in circulation
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + biotin + apo-[propionyl CoA carboxylase]
AMP + diphosphate + propionyl CoA carboxylase
-
-
-
-
?
ATP + biotin + apo-[propionyl-CoA carboxylase]
AMP + diphosphate + propionyl-CoA carboxylase
-
-
-
-
?
ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
AMP + diphosphate + [propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
-
-
-
?
ATP + biotin + histone H4
AMP + diphosphate + biotin-histone H4
-
biotinylation at Lys12 especially in telomeric repeats, overview
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
?
-
plays an essential role in biotin utilization
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
?
-
its deficiency causes biotin-responsive multiple carboxylase deficiency in humans
-
-
?
ATP + biotin + apo-[propanoyl-CoA:carbon-dioxide ligase (ADP-forming)]
?
-
-
-
-
?
additional information
?
-
-
although mammals have multiple biotin-dependent enzymes there is only a single gene encoding holocarboxylase synthetase, HCS, responsible for all cellular biotinylation. The enzyme catalyzes the reactions of EC 6.3.4.10, EC 6.3.4.11, and EC 6.3.4.15, overview
-
-
?
additional information
?
-
-
holocarboxylase synthetase catalyzes the attachment of biotin to the epsilon-amino group of a specific lysine residue in apocarboxylases, biotinylation of biotin-dependent carboxylases requires ATP and proceeds in the following two steps
-
-
?
additional information
?
-
-
holocarboxylase synthetase, HCS, catalyzes the binding of biotin to lysines in carboxylases and histones in two steps. First, HCS catalyzes the synthesis of biotinyl-5'-AMP, and second, the biotinyl moiety is ligated to lysine residues, binding structure, modelling, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the reactions of EC 6.3.4.10, EC 6.3.4.11, and EC 6.3.4.15, overview
-
-
?
additional information
?
-
-
the enzyme is critical to utilization of exogenous or dietary biotin and responds to biotin deprivation by reduction in the steady state level of their mRNAs. The free biotin is directed to brain because the reduction in holocarboxylase synthetase, sodium-dependent multivitamin-transporter and carboxylase mRNAs in liver reduces their capacity to utilize biotin while leaving free biotin in circulation
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
HCS from patients with neonatal biotin-responsive multiple carboxylase deficiency has a higher Km for biotin than normal HCS
-
additional information
additional information
-
steady state kinetic analyses as a function of biotin, ATP, or a minimal biotin-accepting substrate concentration indicate similar behaviors for both isozymes, pre-steady state kinetic analysis of the second half-reaction with p76
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
-
-
brenda
-
1390, 1392, 1393, 701935, 702499, 702952, 703282, 703738, 704972, 705293, 705752, 706629, 713742, 714763, 715997, 715999, 726655, 726859, 728180, 745784
-
-
brenda
holocarboxylase synthetase catalyzes the biotinylation of the four biotin-dependent carboxylases found in human, mitochondrial propionyl-CoA carboxylase, pyruvate carboxylase, beta-methylcrotonyl-CoA carboxylase, and cytosolic acetyl-CoA carboxylase
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
lung fibroblasts, quantitative determination of HCS in wild-type IMR-90 fibroblasts and in those recombinantly overexpressing human telomerase, evaluation as a cell model for investigation of HCS in epigenetic regulation, histone biotinylation in aging cells, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
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HCS migrates to the nucleus at the gastrulation stage. In polytene chromosomes, it is associated to heterochromatin bands where it co-localizes with histone 3 trimethylated at lysine 9 but not with the euchromatin mark histone 3 acetylated at lysine 9. HCS associates with the hsp70 promoter. On heat-shock activation of the hsp70 promoter, HCS is displaced and the promoter region becomes enriched with the TFIIH subunits XPD and XPB and elongating RNA pol I
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additional information
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isozyme subcellular localization, immunofluorescence study, overview
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additional information
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HCS co-localizes with histone H3 in human cells with physical interactions between HCS and H3. The N-terminal and C-terminal domains in HCS participate in H3 binding
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
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biotin deficiency, e.g. occuring in patients with BTD deficiency, in severely malnourished children in developing countries, and in individuals consuming large amounts of raw egg white which contains the protein avidin, has adverse effects on cellular and humoral immune functions, and it can lead to candida dermatitis and presented with absent delayed-hypersensitivity skin-tests responses, IgA deficiency, and subnormal percentages of T-lymphocytes in peripheral blood, overview
malfunction
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defective activity of holocarboxylase synthetase in the biotin cycle causes multiple carboxylase deficiency, MCD, an autosomal recessive metabolic disorder usually in the neonatal or early-onset form
malfunction
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deficiency in human HCS results in decreased activity of the acyl-CoA carboxylase and affects various metabolic processes
malfunction
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holocarboxylase synthetase deficiency causes multiple carboxylase deficiency, phenotypes, overview
malfunction
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holocarboxylase synthetase, HCS, deficiency is an inborn error of biotin metabolism, leading to a multiple carboxylases deficiency. A Japanese male neonate with HCS deficiency received maternal administration of biotin from 33 weeks gestation, acylcarnitine profiles compared to control, phenotype, overview
metabolism
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holocarboxylase synthetase governs the cellular fate of the essential micronutrient biotin, i.e. vitamin H or B7
metabolism
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the enzyme is part of the biotin metabolism in which it catalyses the attachment of biotin to apoenzyme carboxylases
metabolism
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holocarboxylase synthetase catalyzes the binding of the vitamin biotin to histones H3 and H4, thereby creating rare histone biotinylation marks in the epigenome. The enzyme interacts physically with euchromatic histone-lysine N-methyltransferase
physiological function
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biotinylation of lysine residues in histones by holocarboxylase synthetase is an epigenetic diet-dependent mechanism to regulate chromatin structure and gene expression
physiological function
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HCS catalyzes the binding of the vitamin biotin to carboxylases and histones
physiological function
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HCS catalyzes transfer of biotin to biotin-dependent carboxylases, and the enzyme is therefore of fundamental importance for many physiological processes, including fatty acid synthesis, gluconeogenesis, and amino acid catabolism. In addition, the enzyme functions in regulating transcription initiation at several genes that code for proteins involved in biotin metabolism
physiological function
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HCS is responsible for attaching biotin onto the biotin-dependent enzymes that reside in the cytoplasm and mitochondria
physiological function
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HCS co-localizes with histone H3 in human cells with physical interactions between HCS and H3. The N-terminal and C-terminal domains in HCS participate in H3 binding
physiological function