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Information on EC 6.4.1.1 - pyruvate carboxylase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P32327
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6.4.1.1 pyruvate carboxylaseIUBMB Comments
A biotinyl-protein containing manganese (animal tissues) or zinc (yeast). The animal enzyme requires acetyl-CoA.
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Word Map
- 6.4.1.1
- phosphoenolpyruvate
-
gluconeogenesis
-
carboxykinase
- biotin
- oxaloacetate
- acetyl-coa
-
tricarboxylic
-
gluconeogenic
-
anaplerotic
- malate
- citrate
- tca
- co2
-
malic
- pepck
- carboxylases
- astrocyte
- glucose-6-phosphatase
-
biotin-dependent
- acidosis
- propionyl-coa
-
citric
-
krebs
- glutamicum
-
bark
- pine
-
biotin-containing
-
13c-labeled
-
propionyl
-
isotopomer
-
maritime
-
1-13cglucose
- avidin
- hyperammonemia
-
fructose-1,6-diphosphatase
- carboxyltransferase
-
pyrogenic
-
4.1.1.32
-
1,6-bisphosphatase
- holocarboxylase
- transcarboxylase
- biotinidase
-
pyrolytic
- leigh
-
ureagenesis
- medicine
-
glucogenic
- biotechnology
- penicillinase
-
13c-enriched
- pinaster
- synthesis
- 3-methylcrotonyl-coa
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Carboxylase, pyruvate
-
-
-
-
PCB
-
-
-
-
Pyruvic carboxylase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + pyruvate + HCO3- = ADP + phosphate + oxaloacetate
reaction mechanism, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -
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
9014-19-1
-
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 + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
Pyc1 and Pyc2 display different allosteric properties with respect to acetyl CoA activation and aspartate inhibition, with Pyc1 showing a higher degree of cooperativity than Pyc2, even in the absence of aspartate
-
-
?
ATP + pyruvate + HCO3- + H+
ADP + phosphate + oxaloacetate
-
-
-
-
?
additional information
?
-
-
in yeast, two metabolic pathways leading to the production of oxaloacetate are the pyruvate carboxylase-catalysed reaction and the glyoxylate cycle.When yeast is grown on acetate, pyruvate carboxylase-catalysed oxaloacetate formation is repressed but the glyoxylate cycle is active, and vice versa if grown on glucose minimal medium
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
r
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
Pyc1 and Pyc2 display different allosteric properties with respect to acetyl CoA activation and aspartate inhibition, with Pyc1 showing a higher degree of cooperativity than Pyc2, even in the absence of aspartate
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview. The enzyme is allosterically regulated by acetyl-CoA and aspartate
-
-
?
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 + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
Pyc1 and Pyc2 display different allosteric properties with respect to acetyl CoA activation and aspartate inhibition, with Pyc1 showing a higher degree of cooperativity than Pyc2, even in the absence of aspartate
-
-
?
additional information
?
-
-
in yeast, two metabolic pathways leading to the production of oxaloacetate are the pyruvate carboxylase-catalysed reaction and the glyoxylate cycle.When yeast is grown on acetate, pyruvate carboxylase-catalysed oxaloacetate formation is repressed but the glyoxylate cycle is active, and vice versa if grown on glucose minimal medium
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
-
-
r
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
Pyc1 and Pyc2 display different allosteric properties with respect to acetyl CoA activation and aspartate inhibition, with Pyc1 showing a higher degree of cooperativity than Pyc2, even in the absence of aspartate
-
-
?
ATP + pyruvate + HCO3-
ADP + phosphate + oxaloacetate
-
the catalyzed anaplerotic reaction is very important replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways, overview. The enzyme is allosterically regulated by acetyl-CoA and aspartate
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Trinitrobenzenesulfonate
-
acetyl-CoA and adenosine 3',5'-diphosphate protect
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
acetyl-CoA and K+ have no effect on ADP phosphorylation by carbamoyl phosphate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.7
Carbamoyl phosphate
-
pH 7.8, 30°C, C249A mutant, with acetyl-CoA and K+
10.7
Carbamoyl phosphate
-
pH 7.8, 30°C, C249A mutant, without acetyl-CoA and K+
11.3
Carbamoyl phosphate
-
pH 7.8, 30°C, wild-type Pyc1, with acetyl-CoA and K+
12.3
Carbamoyl phosphate
-
pH 7.8, 30°C, wild-type Pyc1, without acetyl-CoA and K+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.043
Carbamoyl phosphate
-
pH 7.8, 30°C, C249A mutant, with acetyl-CoA and K+
0.11
Carbamoyl phosphate
-
pH 7.8, 30°C, wild-type Pyc1, with acetyl-CoA and K+
0.11
Carbamoyl phosphate
-
pH 7.8, 30°C, wild-type Pyc1, without acetyl-CoA and K+
0.13
Carbamoyl phosphate
-
pH 7.8, 30°C, C249A mutant, without acetyl-CoA and K+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
expression of the two isoenzymes is differentially regulated and expressed during different growth conditions, expression of PYC1 and PYC2 is influenced by both the growth phase and carbon source, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
additional information
-
all three functional domains, biotin carboxylase, carboxytransferase and biotin carboxyl carrier protein, are located on a single polypeptide chain, domain structures, overview
tetramer
Glu40 and Glu433 play essential roles in subunit interactions
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E40R
predominant form of mutant E40R is the monomer. Coexpression of mutant forms with wild type Pyc1 shows that mutations causes severe loss of interaction with wild type Pyc1
E433R
predominant form of mutant E433R is the monomer. Coexpression of mutant forms with wild type Pyc1 shows that mutations causes severe loss of interaction with wild type Pyc1
R36E
the R36E is much more susceptible to tetramer dissociation and inactivation than the wild type enzyme. Coexpression of mutant forms with wild type Pyc1 shows that the R36E mutation had no effect on the interaction of these subunits with those of wild type Pyc1
R36E/E433R
predominant form of mutant R36E/E433R is the monomer. Coexpression of mutant forms with wild type Pyc1 shows that mutations causes severe loss of interaction with wild type Pyc1
additional information
additional information
construction of chimeric enzymes of Pyc1 and Pyc2
additional information
construction of chimeric enzymes of Pyc1 and Pyc2
additional information
-
construction of chimeric enzymes of Pyc1 and Pyc2
additional information
construction of chimeric enzymes of Pyc1 and Pyc2
additional information
construction of chimeric enzymes of Pyc1 and Pyc2
additional information
-
construction of chimeric enzymes of Pyc1 and Pyc2
additional information
-
50% down-regulation of the enzyme in the RTG1 and the RTG2 mutants
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
coexpression of pyruvate carboxylase 1 isozyme (Pyc1) with an N-terminal myc tag, together with constructs encoding either the biotin carboxylase domain or the transcarboxylase-biotin carboxyl carrier domain, each with an N-terminal 9-histidine tag
two genes PYC1 and PYC2 located on different chromosomes, expression of PYC1 and PYC2 is influenced by both the growth phase and carbon source, overview
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
coexpression of recombinant pyruvate coarboxylase in BHK-21 cells improves the production of human erythropoietin in a continuously perfused bioreactor
synthesis
-
super-transfection of CHO cells with a mammalian construct bearing codon optimized yeast cytosolic pyruvate carboxylase PYC2 and a strong fusion promoter for optimal expression of PYC2 enzyme in order to control the lactate metabolism of mAb (IgG1-kappa) producing CHO clones. Presence of Pyc2 results in an improved mAb titer up to 5%, galactosylation up to 2.5folds, and mannosylation up to twofold
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Libor, S.M.; Sundaram, T.K.; Scrutton, M.C.
Pyruvate carboxylase from a thermophilic Bacillus
Biochem. J.
169
543-558
1978
Bacillus sp. (in: Bacteria), Saccharomyces cerevisiae, Gallus gallus, Rattus norvegicus
Barden, R.E.; Taylor, B.L.; Isohashi, F.; Frey, W.H.; Zander, G.; Lee, J.C.; Utter, M.F.
Structural properties of pyruvate carboxylase from chicken liver and other sources
Proc. Natl. Acad. Sci. USA
72
4308-4312
1975
Bos taurus, Saccharomyces cerevisiae, Gallus gallus, Homo sapiens, Meleagris gallopavo, Pseudomonas citronellolis, Rattus norvegicus, Sus scrofa
Attwood, P.V.
The structure and the mechanism of action of pyruvate carboxylase
Int. J. Biochem. Cell Biol.
27
231-249
1995
Aspergillus nidulans, Saccharomyces cerevisiae, Gallus gallus, Pseudomonas citronellolis, vertebrata
Chapman-Smith, A.; Booker, G.W.; Clements, P.R.; Wallace, J.C.; Keech, D.B.
Further studies on the localization of the reactive lysyl residue of pyruvate carboxylase
Biochem. J.
276
759-764
1991
Saccharomyces cerevisiae, Ovis aries
Lim, F.; Morris, C.P.; Occhiodora, F.; Wallace, J.C.
Sequence and domain structure of yeast pyruvate carboxylase
J. Biol. Chem.
263
11493-11497
1988
Saccharomyces cerevisiae
Jitrapakdee, S.; Wallace, J.C.
Structure, function and regulation of pyruvate carboxylase
Biochem. J.
340
1-16
1999
Geobacillus stearothermophilus, Saccharomyces cerevisiae, Mammalia, Methanothermobacter thermautotrophicus, Rhizobium etli, Homo sapiens (P11498)
-
Branson, J.P.; Nezic, M.; Wallace, J.C.; Attwood, P.V.
Kinetic characterization of yeast pyruvate carboxylase isozyme pyc1
Biochemistry
41
4459-4466
2002
Saccharomyces cerevisiae
Branson, J.P.; Nezic, M.; Jitrapakdee, S.; Wallace, J.C.; Attwood, P.V.
Kinetic characterization of yeast pyruvate carboxylase isozyme Pyc1 and the Pyc1 mutant, C249A
Biochemistry
43
1075-1081
2004
Saccharomyces cerevisiae
Irani, N.; Beccaria, A.J.; Wagner, R.
Expression of recombinant cytoplasmic yeast pyruvate carboxylase for the improvement of the production of human erythropoietin by recombinant BHK-21 cells
J. Biotechnol.
93
269-282
2002
Saccharomyces cerevisiae
Fogolin, M.B.; Wagner, R.; Etcheverrigaray, M.; Kratje, R.
Impact of temperature reduction and expression of yeast pyruvate carboxylase on hGM-CSF-producing CHO cells
J. Biotechnol.
109
179-191
2004
Saccharomyces cerevisiae
Jitrapakdee, S.; Adina-Zada, A.; Besant, P.G.; Surinya, K.H.; Cleland, W.W.; Wallace, J.C.; Attwood, P.V.
Differential regulation of the yeast isozymes of pyruvate carboxylase and the locus of action of acetyl CoA
Int. J. Biochem. Cell Biol.
39
1211-1223
2007
Saccharomyces cerevisiae (P11154), Saccharomyces cerevisiae (P32327), Saccharomyces cerevisiae, Saccharomyces cerevisiae DM18 (P32327)
Jitrapakdee, S.; Surinya, K.H.; Adina-Zada, A.; Polyak, S.W.; Stojkoski, C.; Smyth, R.; Booker, G.W.; Cleland, W.W.; Attwood, P.V.; Wallace, J.C.
Conserved Glu40 and Glu433 of the biotin carboxylase domain of yeast pyruvate carboxylase I isoenzyme are essential for the association of tetramers
Int. J. Biochem. Cell Biol.
39
2120-2134
2007
Saccharomyces cerevisiae (P11154), Saccharomyces cerevisiae
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
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