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Information on EC 6.4.1.1 - pyruvate carboxylase and Organism(s) Staphylococcus aureus and UniProt Accession A0A0H3JRU9

for references in articles please use BRENDA:EC6.4.1.1
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EC Tree
IUBMB Comments
A biotinyl-protein containing manganese (animal tissues) or zinc (yeast). The animal enzyme requires acetyl-CoA.
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This record set is specific for:
Staphylococcus aureus
UNIPROT: A0A0H3JRU9
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Word Map
The taxonomic range for the selected organisms is: Staphylococcus aureus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
pyruvate carboxylase, pyc, pcase, hppyc1p, pyruvate carboxylase 1, pyc1p, ehpyc1, pyruvic carboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Carboxylase, pyruvate
-
-
-
-
PCB
-
-
-
-
Pyruvic carboxylase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + pyruvate + HCO3- = ADP + phosphate + oxaloacetate
show the reaction diagram
reaction mechanism, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
pyruvate:carbon-dioxide ligase (ADP-forming)
A biotinyl-protein containing manganese (animal tissues) or zinc (yeast). The animal enzyme requires acetyl-CoA.
CAS REGISTRY NUMBER
COMMENTARY hide
9014-19-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + pyruvate + HCO3-
ADP + oxaloacetate + phosphate
show the reaction diagram
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
show the reaction diagram
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
show the reaction diagram
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
additional information
?
-
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 + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
show the reaction diagram
the enzyme catalyzes the biotin-dependent production of oxaloacetate and has important roles in gluconeogenesis, lipogenesis, and other cellular processes
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
show the reaction diagram
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
as MgATP2-, dependent on
biotin
-
dependent on, biotin is covalently attached to a specific lysine residue located about 35 residues from the C-terminus
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
as MgATP2-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.58 - 4.4
pyruvate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.2 - 15.7
pyruvate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7 - 27.2
pyruvate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
tetrameric organization of wild-type and isolated C-terminal region, the PC tetramerization, PT, domain is important for oligomerization, conserved mode of tetramerization
tetramer
-
4 * 120000-130000, alpha4
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with coenzyme A, symmetrical tetramer with one coenzyme A molecule bound to each monomer. Presence of acetyl-CoA promotes a conformation for the dimer of the biotin carboxylase domain of pyruvate carboxylase that might be catalytically more competent
purified enzyme in presence of 5 mM ATP and 5 mM oxaloacetic acid, sitting drop method, room temperature, the reservoir solution contains 20% w/v PEG 3350 and 200 mM ammonium tartrate, X-ray diffraction structure determination and analysis at 2.8 A resolution
pyruvate carboxylase tetramers map asymmetric and symmetric architectures, which are coupled to the consecutive biotin carboxylase and carboxyltransferase enzymatic reactions respectively. The catalytic activity occurs one layer at a time
crystal structure analysis
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A610T
more than 30fold loss in catalytic efficiency
K912T
more than 30fold loss in catalytic efficiency
Q870A
2fold loss in catalytic efficiency
R644A
more than 30fold loss in catalytic efficiency
R644K
more than 30fold loss in catalytic efficiency
S911A
1.5fold loss in catalytic efficiency
T908A
more than 30fold loss in catalytic efficiency
Y651A
more than 30fold loss in catalytic efficiency
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jitrapakdee, S.; St Maurice, M.; Rayment, I.; Cleland, W.W.; Wallace, J.C.; Attwood, P.V.
Structure, mechanism and regulation of pyruvate carboxylase
Biochem. J.
413
369-387
2008
Aquifex aeolicus, Geobacillus thermodenitrificans, Bos taurus, Saccharomyces cerevisiae, Ogataea angusta, Homo sapiens, Methanobacterium sp., Methanococcus sp., Methanosarcina sp., Staphylococcus aureus, Mus musculus, Komagataella pastoris, Pseudomonas sp., Rattus norvegicus, Rhizobium etli
Manually annotated by BRENDA team
Xiang, S.; Tong, L.
Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction
Nat. Struct. Mol. Biol.
15
295-302
2008
Staphylococcus aureus (A0A0H3JRU9), Staphylococcus aureus, Homo sapiens (P11498), Homo sapiens
Manually annotated by BRENDA team
Yu, L.P.; Xiang, S.; Lasso, G.; Gil, D.; Valle, M.; Tong, L.
A symmetrical tetramer for S. aureus pyruvate carboxylase in complex with coenzyme A
Structure
17
823-832
2009
Staphylococcus aureus (A0A0H3JRU9), Staphylococcus aureus
Manually annotated by BRENDA team
Westerhold, L.E.; Bridges, L.C.; Shaikh, S.R.; Zeczycki, T.N.
Kinetic and thermodynamic analysis of acetyl-CoA activation of Staphylococcus aureus pyruvate carboxylase
Biochemistry
56
3492-3506
2017
Staphylococcus aureus (A0A0H3JRU9), Staphylococcus aureus, Staphylococcus aureus ATCC 700699 (A0A0H3JRU9)
Manually annotated by BRENDA team
Lasso, G.; Yu, L.P.; Gil, D.; Lazaro, M.; Tong, L.; Valle, M.
Functional conformations for pyruvate carboxylase during catalysis explored by cryoelectron microscopy
Structure
22
911-922
2014
Staphylococcus aureus (A0A0H3JRU9), Staphylococcus aureus, Staphylococcus aureus ATCC 700699 (A0A0H3JRU9)
Manually annotated by BRENDA team