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Information on EC 6.3.4.14 - biotin carboxylase and Organism(s) Homo sapiens

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EC Tree
     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.4 Other carbon-nitrogen ligases
                6.3.4.14 biotin carboxylase
IUBMB Comments
This enzyme, part of an acetyl-CoA carboxylase complex, acts on a biotin carboxyl-carrier protein (BCCP) that has been biotinylated by EC 6.3.4.15, biotin---[biotin carboxyl-carrier protein] ligase. In some organisms the enzyme is part of a multi-domain polypeptide that also includes the carrier protein (e.g. mycobacteria). Yet in other organisms (e.g. mammals) this activity is included in a single polypeptide that also catalyses the transfer of the carboxyl group from biotin to acetyl-CoA (see EC 6.4.1.2, acetyl-CoA carboxylase).
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This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
biotin carboxylase, accbc, pc-beta, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACC
-
-
-
-
BC
-
-
-
-
biotinoyl domain of acetyl-CoA carboxylase
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Carboxylase, biotin
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amination
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
[biotin carboxyl-carrier protein]-biotin-N6-L-lysine:hydrogencarbonate ligase (ADP-forming)
This enzyme, part of an acetyl-CoA carboxylase complex, acts on a biotin carboxyl-carrier protein (BCCP) that has been biotinylated by EC 6.3.4.15, biotin---[biotin carboxyl-carrier protein] ligase. In some organisms the enzyme is part of a multi-domain polypeptide that also includes the carrier protein (e.g. mycobacteria). Yet in other organisms (e.g. mammals) this activity is included in a single polypeptide that also catalyses the transfer of the carboxyl group from biotin to acetyl-CoA (see EC 6.4.1.2, acetyl-CoA carboxylase).
CAS REGISTRY NUMBER
COMMENTARY hide
9075-71-2
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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-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
additional information
?
-
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mechanism of ACC holoenzyme function, structure of the biotinoyl domain of isozyme ACC2, overview
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + biotin-carboxyl-carrier protein + CO2
ADP + phosphate + carboxybiotin-carboxyl-carrier protein
show the reaction diagram
-
The overall acetyl-CoA carboxylase, ACC, reaction proceeds by a two-step mechanism. The first half-reaction is carried out by the biotin carboxylase and involves the ATP-dependent carboxylation of biotin, in which bicarbonate serves as the CO2 source. The carboxyl transferase catalyzes the second half-reaction in which the carboxyl group is transferred from biotin to acetyl-CoA to produce malonyl-CoA, the biotinoyl domain performs a critical function by transferring the activated carboxyl group from the biotin carboxylase domain to the carboxyl transferase domain, overview
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
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ATP-dependent
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
soraphen A
macrocyclic polyketide natural product, binds to the binding site of phosphorylated Ser222, implying that its inhibition mechanism is the same as that of phosphorylation by AMP-activated protein kinase
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACACB_HUMAN
2458
1
276541
Swiss-Prot
-
ACACA_HUMAN
2346
0
265554
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
3D structure of the hACC2 biotinoyl domain, geometry of the consensus Met-Lys-Met, MKM, motif, overview. The biotin group of hACC2 does not affect the structure of the biotinoyl domain, the human enzyme does not possess a thumb structure. Binding pattern and interacting surfaces for the ACC2 biotinoyl domain with Escherichia coli BirA enzyme, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of the biotin carboxylase domain of human acetyl-CoA carboxylase ACC2 phosphorylated by AMP-activated protein kinase AMPK. The phosphorylated Ser222 binds to the putative dimer interface of biotin carboxylase, disrupting polymerization and providing the molecular mechanism of inactivation by AMPK. The structure of the biotin carboxylase domain in complex with soraphen A, a macrocyclic polyketide natural product, shows that the compound binds to the binding site of phosphorylated Ser222, implying that its inhibition mechanism is the same as that of phosphorylation by AMPK
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
V927A/I931M/M932N/T933Q
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site-directed mutagenesis, substitution of four amino acids in the vicinity of human MKM motif in analogy to the Escherichia coli biotinylation site
additional information
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identification of mutations of the pyruvate carboxylase gene that cause pyruvate carboxylase deficiency. Deficiency form A results from association of two missense mutations located in biotin carboxylase or carboxyltransferase N-terminal part domains. Although most pyruvate carboxylase mutations are suggested to interfere with biotin metabolism, none of the pyruvate carboxylase-deficient patients tested is biotin-responsive
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant His-tagged biotinoyl domains from Escherichia coli strain AVB101 by nickel affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant His-tagged biotinoyl domains in Escherichia coli strain AVB101
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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identification of mutations of the pyruvate carboxylase gene that cause pyruvate carboxylase deficiency. Deficiency form A results from association of two missense mutations located in biotin carboxylase or carboxyltransferase N-terminal part domains. Although most pyruvate carboxylase mutations are suggested to interfere with biotin metabolism, none of the pyruvate carboxylase-deficient patients tested is biotin-responsive
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lee, C.K.; Cheong, H.K.; Ryu, K.S.; Lee, J.I.; Lee, W.; Jeon, Y.H.; Cheong, C.
Biotinoyl domain of human acetyl-CoA carboxylase: Structural insights into the carboxyl transfer mechanism
Proteins
72
613-624
2008
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Cho, Y.S.; Lee, J.I.; Shin, D.; Kim, H.T.; Jung, H.Y.; Lee, T.G.; Kang, L.W.; Ahn, Y.J.; Cho, H.S.; Heo, Y.S.
Molecular mechanism for the regulation of human ACC2 through phosphorylation by AMPK
Biochem. Biophys. Res. Commun.
391
187-192
2010
Homo sapiens (O00763), Homo sapiens
Manually annotated by BRENDA team
Monnot, S.; Serre, V.; Chadefaux-Vekemans, B.; Aupetit, J.; Romano, S.; De Lonlay, P.; Rival, J.M.; Munnich, A.; Steffann, J.; Bonnefont, J.P.
Structural insights on pathogenic effects of novel mutations causing pyruvate carboxylase deficiency
Hum. Mutat.
30
734-740
2009
Homo sapiens
Manually annotated by BRENDA team