Information on EC 4.1.1.31 - phosphoenolpyruvate carboxylase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
4.1.1.31
-
RECOMMENDED NAME
GeneOntology No.
phosphoenolpyruvate carboxylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
phosphate + oxaloacetate = phosphoenolpyruvate + HCO3-
show the reaction diagram
-
-
-
-
phosphate + oxaloacetate = phosphoenolpyruvate + HCO3-
show the reaction diagram
rapid equilibrium random bi bi mechanism with a dead end complex enzyme-bicarbonate
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
carboxylation
-
-
-
-
carboxylation
O82072
-
decarboxylation
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
C4 photosynthetic carbon assimilation cycle, NAD-ME type
-
C4 photosynthetic carbon assimilation cycle, NADP-ME type
-
C4 photosynthetic carbon assimilation cycle, PEPCK type
-
Carbon fixation in photosynthetic organisms
-
Carbon fixation pathways in prokaryotes
-
CO2 fixation into oxaloacetate (anapleurotic)
-
ethylene biosynthesis V
-
formaldehyde assimilation I (serine pathway)
-
gluconeogenesis II (Methanobacterium thermoautotrophicum)
-
glutamine biosynthesis III
-
Metabolic pathways
-
Methane metabolism
-
Methanobacterium thermoautotrophicum biosynthetic metabolism
-
Microbial metabolism in diverse environments
-
mixed acid fermentation
-
Pyruvate metabolism
-
reductive TCA cycle I
-
respiration (anaerobic)
-
TCA cycle VI (obligate autotrophs)
-
SYSTEMATIC NAME
IUBMB Comments
phosphate:oxaloacetate carboxy-lyase (adding phosphate; phosphoenolpyruvate-forming)
This enzyme replenishes oxaloacetate in the tricarboxylic acid cycle when operating in the reverse direction. The reaction proceeds in two steps: formation of carboxyphosphate and the enolate form of pyruvate, followed by carboxylation of the enolate and release of phosphate.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
archaeal-type phosphoenolpyruvate carboxylase
Q8XLE8
-
atPEPC
Q97WG4
-
-
Atppc1
Q9MAH0
-
Atppc2
Q5GM68
-
Atppc3
Q84VW9
-
Atppc4
Q8GVE8
-
bacterial-type PEPC
A6YM33
-
bacterial-type phosphoenolpyruvate carboxylase
-
-
bacterial-type phosphoenolpyruvate carboxylase
-
-
bacterial-type phosphoenolpyruvate carboxylase
-
-
bacterial-type phosphoenolpyruvate carboxylase
-
-
BTPC
A6YM33
-
C4-PEPC
-
-
Carboxylase, phosphopyruvate (phosphate)
-
-
-
-
Class-1 PEPC
-
-
Class-2 PEPC
-
-
CP21
-
-
-
-
CP28
-
-
-
-
CP46
-
-
-
-
Ljpepc1
-
-
Osppc2a
-
isoform
Osppc4
-
isoform
PEP carboxylase
-
-
-
-
PEP carboxylase
-
-
PEP carboxylase
-
-
PEP carboxylase
-
-
PEP-carboxylase
-
-
PEP-carboxylase
-
-
PEPC
-
-
-
-
PEPC
Amaranthus edulis
-
-
PEPC
Q5GM68, Q84VW9, Q8GVE8, Q9MAH0
-
PEPC
P81831, Q6R2V6
-
PEPC
Musa cavendishii
-
-
PEPC
A6YM33
-
PEPC
Salsola richteri
-
-
PEPC
O82072
-
PEPC(p102)kinase
-
-
PEPC1
-
isozyme
PEPC1
-
isoform
PEPC2
-
isoform
PEPC7
-
isoform
PEPCase
-
-
-
-
PEPCase
Q1XAT8
-
PEPCase
Q1XAT9
-
PEPCase
Q1XAT7
-
PEPCase
-
-
phosphoenol pyruvate carboxylase
-
-
phosphoenolpyruvate carboxykinase
-
-
Phosphoenolpyruvate carboxylase
-
-
-
-
Phosphoenolpyruvate carboxylase
-
-
Phosphoenolpyruvate carboxylase
-
-
Phosphoenolpyruvate carboxylase
-
-
Phosphoenolpyruvate carboxylase
-
-
Phosphoenolpyruvate carboxylase
-
-
Phosphoenolpyruvate carboxylase
-
-
Phosphoenolpyruvate carboxylase
-
-
Phosphoenolpyruvate carboxylase
-
-
Phosphoenolpyruvate carboxylase
-
-
Phosphoenolpyruvate carboxylase
-
-
Phosphoenolpyruvate carboxylase
-
-
Phosphoenolpyruvate carboxylase
-
-
Phosphoenolpyruvate carboxylase
-
-
Phosphoenolpyruvate carboxylase
-
-
Phosphoenolpyruvate carboxylase
-
-
Phosphoenolpyruvate carboxylase
-
-
Phosphoenolpyruvate carboxylase
Pseudomonas aeruginosa P4
-
-
-
Phosphoenolpyruvate carboxylase
-
-
Phosphoenolpyruvate carboxylase
A6YM33
-
Phosphoenolpyruvate carboxylase
-
-
Phosphoenolpyruvate carboxylase
Salsola richteri
-
-
Phosphoenolpyruvate carboxylase
-
-
Phosphoenolpyruvate carboxylase
-
-
Phosphoenolpyruvate carboxylase
-
-
Phosphoenolpyruvate carboxylase
O82072
-
Phosphoenolpyruvic carboxylase
-
-
-
-
photosynthetic phosphoenolpyruvate carboxylase
-
-
plant-type phosphoenolpyruvate carboxylase
-
-
plant-type phosphoenolpyruvate carboxylase
-
-
plant-type phosphoenolpyruvate carboxylase
-
-
plant-type phosphoenolpyruvate carboxylase
-
-
plant-type phosphoenolpyruvate carboxylase
-
-
PPC
Bradyrhizobium japonicum USDA110
-
-
-
PPC
Pseudomonas aeruginosa P4
-
-
-
PPC
A6YM33
-
PPC1
-
isozyme
PPCK1
-
isozyme
PPCK2
-
isozyme
S.minutum PEPC1
-
-
SSO2256
Q97WG4
locus name
SSO2256
Q97WG4
locus name
-
CAS REGISTRY NUMBER
COMMENTARY
9067-77-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
-
Q1XAT7
SwissProt
Manually annotated by BRENDA team
Amaranthus edulis
-
-
-
Manually annotated by BRENDA team
cultivar AG-67
-
-
Manually annotated by BRENDA team
cultivar Landsberg erecta
-
-
Manually annotated by BRENDA team
ecotype Columbia 0
-
-
Manually annotated by BRENDA team
ecotype Wassilevskija
-
-
Manually annotated by BRENDA team
photosynthetic type: single cell C4
-
-
Manually annotated by BRENDA team
hybrid cv. Mulato
-
-
Manually annotated by BRENDA team
Bradyrhizobium japonicum USDA110
-
-
-
Manually annotated by BRENDA team
Bryophyllum fedtschenkoi
-
-
-
Manually annotated by BRENDA team
strain CW-15 cc1883
-
-
Manually annotated by BRENDA team
Chlamydomonas reinhardtii CW-15 cc1883
strain CW-15 cc1883
-
-
Manually annotated by BRENDA team
variant Valencia
-
-
Manually annotated by BRENDA team
variant Valencia late
-
-
Manually annotated by BRENDA team
Coccochloris peniocystis
-
-
-
Manually annotated by BRENDA team
Crassula argentea
-
-
-
Manually annotated by BRENDA team
; wild type and mutant enzymes Arg703Gly and Arg703Gly/Arg704Gly
Uniprot
Manually annotated by BRENDA team
strain B
-
-
Manually annotated by BRENDA team
strain K-12
-
-
Manually annotated by BRENDA team
strain W
-
-
Manually annotated by BRENDA team
cultivar Williams
-
-
Manually annotated by BRENDA team
cultivar Coker 315
Uniprot
Manually annotated by BRENDA team
photosynthetic type: Kranz C4
-
-
Manually annotated by BRENDA team
L.f. Royle
-
-
Manually annotated by BRENDA team
cultivar Hinomoto
-
-
Manually annotated by BRENDA team
golden delicious, cox's orange Pippin
-
-
Manually annotated by BRENDA team
Molinema dessetae
-
-
-
Manually annotated by BRENDA team
green alga
-
-
Manually annotated by BRENDA team
Musa cavendishii
-
-
-
Manually annotated by BRENDA team
cultivar Tsukinohikari
-
-
Manually annotated by BRENDA team
Panicum schenckii
-
-
-
Manually annotated by BRENDA team
strain P4 (soil-isolate)
-
-
Manually annotated by BRENDA team
Pseudomonas aeruginosa P4
strain P4 (soil-isolate)
-
-
Manually annotated by BRENDA team
strain ATCC 13525
-
-
Manually annotated by BRENDA team
strain No.7
-
-
Manually annotated by BRENDA team
cultivar Baker 296
-
-
Manually annotated by BRENDA team
L. Cv. Baker 296
-
-
Manually annotated by BRENDA team
L. var. Baker 296
-
-
Manually annotated by BRENDA team
Salsola richteri
photosynthetic type: Kranz C4
-
-
Manually annotated by BRENDA team
sorghum C4 isoform
Uniprot
Manually annotated by BRENDA team
var. Tamaran
-
-
Manually annotated by BRENDA team
Sorghum sp.
-
-
-
Manually annotated by BRENDA team
strain ATCC 90893
-
-
Manually annotated by BRENDA team
strain A3(2)
-
-
Manually annotated by BRENDA team
photosynthetic type: single cell C4
-
-
Manually annotated by BRENDA team
photosynthetic type: Kranz C4
-
-
Manually annotated by BRENDA team
photosynthetic type: C3
-
-
Manually annotated by BRENDA team
different winter wheat genotypes (P16, LK5029, ND139, 93-9, J5385, 95021, HXM16, C030, GY503, H5316, NDF270, DK90, N341, C026, YN15, 6365)
UniProt
Manually annotated by BRENDA team
L. cv. Chineses Spring
-
-
Manually annotated by BRENDA team
variant PBW-343
-
-
Manually annotated by BRENDA team
-
Uniprot
Manually annotated by BRENDA team
3 enzyme forms: root-form PEPC, C4-form PEPC, C3-housekeeping form PEPC
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
Amaranthus edulis
-
the deficiency in C4 PEPC in mutant LaC4 2.16 Amaranthus edulis leaves has no effect on C3-type PEPC content and phosphorylation state in seeds, but causes impairment of energy production, thereby accounting for the reduced germination of the mutant
physiological function
-, O23946
PEPC is a key enzyme in the synthesis of malate
physiological function
-
PEPC is involved in atmospheric CO2 fixation, C/N interaction and anaplerotic C-flux, energy supply for symbiotic bacteria, carbon storage in cell vacuoles, root malate/citrate excretion for abiotic stress acclimation, seed germination, seed development, and cell expansion
physiological function
-
PEPC is involved in atmospheric CO2 fixation, C/N interaction and anaplerotic C-flux, energy supply for symbiotic bacteria, carbon storage in cell vacuoles, root malate/citrate excretion for abiotic stess acclimation, seed germination, seed development, and cell expansion
physiological function
-
PEPC is involved in atmospheric CO2 fixation, C/N interaction and anaplerotic C-flux, energy supply for symbiotic bacteria, carbon storage in cell vacuoles, root malate/citrate excretion for abiotic stress acclimation, seed germination, seed development, and cell expansion
physiological function
-
BTPC accelerates the metabolic flow for the synthesis of storage substances during pollen maturation
physiological function
-
Bradyrhizobium japonicum utilizes PPC as an anaplerotic enzyme for growth on carbon sources metabolized to three-carbon intermediates
physiological function
-
the phosphorylation status and the protein levels of PEPC are crucial in modulating the daily and seasonal patterns in C4 leaves in situ
physiological function
-
BTPC and thus class-2 PEPC up-regulation is a distinctive feature of rapidly growing and/or biosynthetically active tissues that require a large anaplerotic flux from phosphoenolpyruvate to replenish tricarboxylic acid cycle C-skeletons being withdrawn for anabolism
physiological function
-
the enzyme is suited for organic acid synthesis and NADH reoxidation in the mature fruit
physiological function
Bradyrhizobium japonicum USDA110
-
Bradyrhizobium japonicum utilizes PPC as an anaplerotic enzyme for growth on carbon sources metabolized to three-carbon intermediates
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
phosphate + oxaloacetate
H2O + phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
?
phosphate + oxaloacetate
phosphoenolpyruvate + CO2
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
P00864
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
P00864
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
ir
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
P27154
-
-
-
ir
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
ir
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
ir
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
P15804
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
ir
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-, O23946
-
-
-
ir
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
ir
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
Bryophyllum fedtschenkoi
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
Bryophyllum fedtschenkoi
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
Bryophyllum fedtschenkoi
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
Bryophyllum fedtschenkoi
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
Coccochloris peniocystis
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
Crassula argentea
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
Crassula argentea
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
Sorghum sp.
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
Amaranthus edulis
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
P0A3X6, -
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
Q1XAT9
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
Q1XAT8
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-, Q1XAT7
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
Q5GM68, Q84VW9, Q8GVE8, Q9MAH0
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
O82072
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
A6YM33
-
-
-
ir
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
Q97WG4, -
-
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
Molinema dessetae
-
enzyme does not catalyze the reverse reaction
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
by shifting to CAM in the C4 Portulaca a nes PEPC isoform may be synthesized to meet CAM requirements
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
key enzyme in fixation of atmospheric CO2 in C4 and crassulacean acid metabolism
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-, Q9M3Y3
moderated water stress applied to Pinus halepensis has no effect on PEPC activity. Ozone stress induces a dramatic increase of PEPC activity in pine needles
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
NaCl and LiCl induce enzyme expression in roots. Other abiotic stresses affecting water status, such as drought or cold, induce PEPC expression. Important role of the enzyme in the adaption of plants to environmental changes
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
the enzyme is responsible for primary CO2 fixation. PEPC activity and regulationm are modified upon drought stress treatment in a way that allows Portulaca oleracea to perform a CAM-like metabolism
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
the organism expresses, regulates and assembles divergent PEPC polypeptides. This probably serves an adaptive pupose by posing these organism for survival in different environments varying in nutrient content
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
concerted sequential allosteric mechanism
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
Rhodopseudomonas sp. No. 7
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
Chlamydomonas reinhardtii CW-15 cc1883
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
Q97WG4
-
-
-
?
Phosphoenolpyruvate + CO2
?
show the reaction diagram
Molinema dessetae
-
enzyme at the branchpoint of glycolysis and Krebs cycle
-
-
-
Phosphoenolpyruvate + CO2
?
show the reaction diagram
-
key enzyme in the supply of carbon skeleton for the assimilation of nitrogen by green algae
-
-
-
Phosphoenolpyruvate + CO2
?
show the reaction diagram
-
function is probably anaplerotic
-
-
-
Phosphoenolpyruvate + CO2
?
show the reaction diagram
-
key enzyme mediating the primary carbon assimilation
-
-
-
Phosphoenolpyruvate + CO2
?
show the reaction diagram
-
three PEPC isoforms: one is the C4-form PEPC, which plays a cardinal role in the initial CO2-fixation of C4 photosynthesis by capturing atmospheric CO2 into C4-dicarboxylic acids, the second one is a C3-housekeeping PEPC, which plays anaplerotic roles by replenishing C4-dicarboxylic acids in the citric acid cycle for synthesis of cell constituents, the root-form PEPC plays various anaplerotic roles, including providing the carbon skeletons for nitrogen assimilation, pH maintenance, and osmolarity regulation
-
-
-
Phosphoenolpyruvate + CO2
?
show the reaction diagram
Bryophyllum fedtschenkoi
-
possible role of the enzyme in controlling a circadian rhythm of CO2 fixation
-
-
-
Phosphoenolpyruvate + CO2
?
show the reaction diagram
-
in C4 plants the enzyme catalyzes the first step of the C4 dicarboxylic acid pathway. In CAM plants the enzyme functions in CO2 fixation
-
-
-
Phosphoenolpyruvate + CO2
?
show the reaction diagram
-
Umbilicus rupestris switches from C3 photosynthesis to an incomplete form of crassulacean acid metabolism, referred to as CAM-idling, when exposed to water stress. This switch is accompanied by an increase in the activity of phosphoenolpyruvate carboxylase
-
-
-
Phosphoenolpyruvate + CO2
?
show the reaction diagram
-
key enzyme in CO2 assimilation pathway of C4 and CAM plants
-
-
-
Phosphoenolpyruvate + CO2
?
show the reaction diagram
-
the enzyme is involved in autotrophic CO2 fixation
-
-
-
Phosphoenolpyruvate + CO2
?
show the reaction diagram
Chlamydomonas reinhardtii CW-15 cc1883
-
key enzyme in the supply of carbon skeleton for the assimilation of nitrogen by green algae
-
-
-
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
P00864
-
-
-
-
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
-
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
-
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
-
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
-
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
r
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
-
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
-
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
-
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
-
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
-
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
-
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
-
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
Coccochloris peniocystis
-
-
-
-
-
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
-
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
?, ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
Molinema dessetae
-
-
-
-
-
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
-
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
Amaranthus edulis
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
Musa cavendishii
-
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-, Q8XLE8
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
feeding K+ or Na+ nitrate salts in vivo enhances the activity of the enzyme in the leaf extract of the C3 plant
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
feeding K+ or Na+ nitrate salts in vivo enhances the activity of the enzyme in the leaf extract of the C4 plant
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
it is suggested that Ca2+ regulates PEPC, at an upstream level, such as transcription, by modulating PEPC-protein kinase, thus facilitating the light activation of PEPC
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
PEPC plays a role in respiratory carbon dioxide refixation while generating malate to support amino acid and/or fatty acids biosynthesis
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
Pseudomonas aeruginosa P4
-
-
-
-
r
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
Rhodopseudomonas sp. No. 7
-
-
-
-
-
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
Bradyrhizobium japonicum USDA110
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
-
additional information
?
-
-
the guard cell enzyme is regulated by reversible phosphorylation of at least one isoform
-
-
-
additional information
?
-
O82072
PEPC may be involved in protein biosynthesis during grain development, and it may have an important role in regulating carbon and nitrogen metabolism in the ear organ of wheat
-
-
-
additional information
?
-
A6YM33
recombinant PPC4 forms class-2 PEPC when combined with class-1 PEPCs
-
-
-
additional information
?
-
-
BTPC tightly interacts with co-expressed PTPC to form the allosterically-desensitized class-2 PEPC heteromeric complex
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
by shifting to CAM in the C4 Portulaca a nes PEPC isoform may be synthesized to meet CAM requirements
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
key enzyme in fixation of atmospheric CO2 in C4 and crassulacean acid metabolism
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-, Q9M3Y3
moderated water stress applied to Pinus halepensis has no effect on PEPC activity. Ozone stress induces a dramatic increase of PEPC activity in pine needles
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
NaCl and LiCl induce enzyme expression in roots. Other abiotic stresses affecting water status, such as drought or cold, induce PEPC expression. Important role of the enzyme in the adaption of plants to environmental changes
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
the enzyme is responsible for primary CO2 fixation. PEPC activity and regulationm are modified upon drought stress treatment in a way that allows Portulaca oleracea to perform a CAM-like metabolism
-
-
?
phosphoenolpyruvate + CO2
phosphate + oxaloacetate
show the reaction diagram
-
the organism expresses, regulates and assembles divergent PEPC polypeptides. This probably serves an adaptive pupose by posing these organism for survival in different environments varying in nutrient content
-
-
?
Phosphoenolpyruvate + CO2
?
show the reaction diagram
Molinema dessetae
-
enzyme at the branchpoint of glycolysis and Krebs cycle
-
-
-
Phosphoenolpyruvate + CO2
?
show the reaction diagram
-
key enzyme in the supply of carbon skeleton for the assimilation of nitrogen by green algae
-
-
-
Phosphoenolpyruvate + CO2
?
show the reaction diagram
-
function is probably anaplerotic
-
-
-
Phosphoenolpyruvate + CO2
?
show the reaction diagram
-
key enzyme mediating the primary carbon assimilation
-
-
-
Phosphoenolpyruvate + CO2
?
show the reaction diagram
-
three PEPC isoforms: one is the C4-form PEPC, which plays a cardinal role in the initial CO2-fixation of C4 photosynthesis by capturing atmospheric CO2 into C4-dicarboxylic acids, the second one is a C3-housekeeping PEPC, which plays anaplerotic roles by replenishing C4-dicarboxylic acids in the citric acid cycle for synthesis of cell constituents, the root-form PEPC plays various anaplerotic roles, including providing the carbon skeletons for nitrogen assimilation, pH maintenance, and osmolarity regulation
-
-
-
Phosphoenolpyruvate + CO2
?
show the reaction diagram
Bryophyllum fedtschenkoi
-
possible role of the enzyme in controlling a circadian rhythm of CO2 fixation
-
-
-
Phosphoenolpyruvate + CO2
?
show the reaction diagram
-
in C4 plants the enzyme catalyzes the first step of the C4 dicarboxylic acid pathway. In CAM plants the enzyme functions in CO2 fixation
-
-
-
Phosphoenolpyruvate + CO2
?
show the reaction diagram
-
Umbilicus rupestris switches from C3 photosynthesis to an incomplete form of crassulacean acid metabolism, referred to as CAM-idling, when exposed to water stress. This switch is accompanied by an increase in the activity of phosphoenolpyruvate carboxylase
-
-
-
Phosphoenolpyruvate + CO2
?
show the reaction diagram
-
key enzyme in CO2 assimilation pathway of C4 and CAM plants
-
-
-
Phosphoenolpyruvate + CO2
?
show the reaction diagram
-
the enzyme is involved in autotrophic CO2 fixation
-
-
-
Phosphoenolpyruvate + CO2
?
show the reaction diagram
Chlamydomonas reinhardtii CW-15 cc1883
-
key enzyme in the supply of carbon skeleton for the assimilation of nitrogen by green algae
-
-
-
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
-
-
ir
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
feeding K+ or Na+ nitrate salts in vivo enhances the activity of the enzyme in the leaf extract of the C3 plant
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
feeding K+ or Na+ nitrate salts in vivo enhances the activity of the enzyme in the leaf extract of the C4 plant
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
it is suggested that Ca2+ regulates PEPC, at an upstream level, such as transcription, by modulating PEPC-protein kinase, thus facilitating the light activation of PEPC
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
-
PEPC plays a role in respiratory carbon dioxide refixation while generating malate to support amino acid and/or fatty acids biosynthesis
-
-
?
phosphoenolpyruvate + HCO3-
phosphate + oxaloacetate
show the reaction diagram
Bradyrhizobium japonicum USDA110
-
-
-
-
?
additional information
?
-
-
the guard cell enzyme is regulated by reversible phosphorylation of at least one isoform
-
-
-
additional information
?
-
O82072
PEPC may be involved in protein biosynthesis during grain development, and it may have an important role in regulating carbon and nitrogen metabolism in the ear organ of wheat
-
-
-
additional information
?
-
A6YM33
recombinant PPC4 forms class-2 PEPC when combined with class-1 PEPCs
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
acetyl-CoA
-
activates
acetyl-CoA
-
absolute requirement for acetyl-CoA or propionyl-CoA
acetyl-CoA
-
no effect
acetyl-CoA
-
strongly dependent on the allosteric activator
acetyl-CoA
-
activates
acetyl-CoA
-
no effect
NADPH
Coccochloris peniocystis
-
activates
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Cd2+
-
28% of the activation with Mg2+
Co2+
-
divalent cation required, Mn2+, Co2+ and Mg2+. Co2+ is less effective than Mg2+ or Mn2+; Km: 0.26 mM; maximal activity at 1 mM Co2+, strong decrease of activity above 4 mM
Co2+
Coccochloris peniocystis
-
60% of the activation with Mg2+
Co2+
-
divalent cation required, Mn2+, Co2+ and Mg2+. Co2+ is less effective than Mg2+ or Mn2+
Co2+
-
30% of the activation with Mg2+
Co2+
-
18% of the activation with Mg2+
Co2+
-, Q8XLE8
PepcA catalyzes formation of oxaloacetate in the presence of Mg2+, Mn2+, or Co2+ but not in the absence of a divalent metal ion
Fe2+
-
12% of the activation with Mg2+
K+
-
12 mM, stimulates by 40%
Mg2+
-
Km: 1.3 mM
Mg2+
-
activates
Mg2+
-
Km: 0.37 mM
Mg2+
-
activates; Km for isoenzyme PC-I: 0.032 mM; Km for isoenzyme PC-II: 0.015 mM
Mg2+
-
divalent cation required, Mn2+, Co2+ and Mg2+; Km: 0.77 mM
Mg2+
-
Km: 0.8 mM; required
Mg2+
-
Km: 0.1 mM
Mg2+
-
Km: 0.56 mM; required
Mg2+
-
activates
Mg2+
Coccochloris peniocystis
-
activates; Km: 0.27 mM
Mg2+
-
divalent cation required, Mn2+, Co2+ and Mg2+
Mg2+
-
activates; Km: 0.8 mM
Mg2+
-
activates; half-maximal activity at 0.1 mM; Km: 0.1 mM
Mg2+
-
activates
Mg2+
-
activates; desensitization by bicarbonate
Mg2+
-
absolute requirement for divalent cation is satisfied by Mg2+
Mg2+
P00864
activates; Km: 1.5 mM
Mg2+
Molinema dessetae
-
Mg2+ or Mn2+ required
Mg2+
-
divalent cation required, Mg2+ is the best activator
Mg2+
-
Mg2+ or Mn2+ required
Mg2+
-
divalent cation required, Mg2+ is the best activator
Mg2+
-
p102 phosphorylation is absolutely dependent upon the presence of MgCl2
Mg2+
-
absolute dependence for a divalent cation, Km: 0.084 mM
Mg2+
-
KM-value for the enzyme from roots grown in presence of Fe2+ is 0.93 mM, The KM-value from enzyme grown in absence of Fe2+ is 0.91 mM
Mg2+
-
-
Mg2+
Amaranthus edulis
-
-
Mg2+
-
absolute dependence
Mg2+
A6YM33
absolutely dependent on, PPC4 exhibits a 4fold higher specific activity with saturating (10mM) Mg2+ relative to Mn2+
Mg2+
-, O23946
required
Mg2+
-
required
Mg2+
-, Q8XLE8
required for activity, PepcA catalyzes formation of oxaloacetate in the presence of Mg2+, Mn2+, or Co2+ but not in the absence of a divalent metal ion
Mg2+
-
the enzyme absolutely requires Mg2+ and cannot utilize Mn2+ instead, maximal activity at 1 mM, decrease of activity at higher concentrations
Mg2+
Q97WG4, -
the enzyme activity is completely dependent on the presence of Mg2+. The enzyme activity could not be reconstituted by the addition of Mn2+ instead of Mg2+
Mn2+
-
activates
Mn2+
-
Km for isoenzyme PC-I: 0.0102 mM; Km for isoenzyme PC-II: 0.0067 mM
Mn2+
-
divalent cation required, Mn2+, Co2+ and Mg2+; Km: 0.12 mM; maximal activity at 0.5 mM Mn2+, strong decrease of activity above 2 mM
Mn2+
-
no activation
Mn2+
-
activates
Mn2+
Coccochloris peniocystis
-
80% of the activation with Mg2+
Mn2+
-
activates
Mn2+
Molinema dessetae
-
Mg2+ or Mn2+ required
Mn2+
-
68% of the activation with Mg2+. At suboptimal concentrations of phosphoenolpyruvate and HCO3-, Mn2+ is more effective than Mg2+
Mn2+
-
Mg2+ or Mn2+ required
Mn2+
-
23% of the activation with Mg2+
Mn2+
-
absolute dependence
Mn2+
A6YM33
may replace Mg2+
NaCl
Coccochloris peniocystis
-
activation between 25 and 200 mM to a maximum of 14% a at 75 mM
phosphate
-
activates
phosphate
Bryophyllum fedtschenkoi
-
the night form of the enzyme is phosphorylated, the phosphate is covalently bound to Ser, the day form of the enzyme is dephosphorylated
phosphate
-
activates at pH 7 in absence of glycerol, inhibits under other assay conditions
phosphate
-
the enzyme from root is phosphorylated by both mammalian cAMP-dependent protein kinase and maize leaf protein kinase, the phosphorylated enzyme is less sensitive to malate
Zn2+
Coccochloris peniocystis
-
60% of the activation with Mg2+
Mn2+
-, Q8XLE8
PepcA catalyzes formation of oxaloacetate in the presence of Mg2+, Mn2+, or Co2+ but not in the absence of a divalent metal ion
additional information
-
feeding K+ or Na+ nitrate salts in vivo enhances the activity of the enzyme in the leaf extract
additional information
-
Cd2 + toxicity leads to PEPC up-regulation, iron deficiency also up-regulates PEPC activity
additional information
-
Cd2+ toxicity leads to PEPC up-regulation, iron deficiency also up-regulates PEPC activity
additional information
-
Cd2 + toxicity leads to PEPC up-regulation, iron deficiency also up-regulates PEPC activity
additional information
-
Cd2+ toxicity leads to PEPC up-regulation, iron deficiency also up-regulates PEPC activity
additional information
-
Cd2 + toxicity leads to PEPC up-regulation, iron deficiency also up-regulates PEPC activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-oxoglutarate
-
-
2-oxoglutarate
-
-
2-oxoglutarate
Coccochloris peniocystis
-
-
2-oxoglutarate
-
isoenzyme PEPC1 is more sensitive to inhibition than isoenzyme PEPC2
2-oxoglutarate
-
potent inhibitor at pH 7 in absence of glycerol, but its effectiveness is decreased by raising the pH to 8 and/or by adding glycerol
2-oxoglutarate
-
inhibition of enzyme form PEPC I and PEPC II, no inhibition of enzyme form PEPC III
2-phosphoglycerate
-
-
3-Mercaptopropionate
-
-
3-phosphoglycerate
-
-
ADP
-
competitive
ADP
-
10mM, 57% inhibition in presence of 5 mM Mg2+, 46% inhibition in presence of 15 mM Mg2+
alpha-Hydroxy-2-pyridylmethanesulfonate
Coccochloris peniocystis
-
-
alpha-ketoglutarate
P0A3X6, -
10 mM, 9% inhibition
AMP
-
10mM, 16% inhibition in presence of 5 mM Mg2+, 12% inhibition in presence of 15 mM Mg2+
Asp
-
L-Asp, competitive
Asp
-
isoenzyme PEPC1 is more sensitive to inhibition than isoenzyme PEPC2
Asp
-
potent inhibitor at pH 7 in absence of glycerol, but its effectiveness is decreased by raising the pH to 8 and/or by adding glycerol
Asp
-
at pH 7.2, weak competitive inhibition for enzyme form PEPC I, strong competitive inhibition for enzyme form PEPC II and enzyme form PEPC III
aspartate
-
-
aspartate
-
IC50 of phospho-PEPC1: 0.35 mM, IC50 of dephospho-PEPC1: 0.32 mM; IC50 of phospho-PEPC2: 2.6 mM, IC50 of dephospho-PEPC2: 4.5 mM, enzyme form PEPC2
ATP
-
competitive
ATP
Coccochloris peniocystis
-
-
ATP
-
2 mM, 65% decreases of activity of PEPC1 at pH 7.3, 13% decrease in activity of PEPC2 at pH 8
ATP
P0A3X6, -
5.0 mM, 57% inhibition
ATP
-
10mM, 92% inhibition in presence of 5 mM Mg2+, 65% inhibition in presence of 15 mM Mg2+
Ca2+
-
substitution of 20 mM CaCl2 for 20 mM MgCl2 results in 90-100% inhibition
Ca2+
-
5 mM, in presence of 5 mM Mg2+, 83% inhibition
Cd2+
-
5 mM, in presence of 5 mM Mg2+
Cd2+
Molinema dessetae
-
-
Chloroquine
-
-
citrate
-
-
citrate
Coccochloris peniocystis
-
-
citrate
-
potent inhibitor at pH 7 in absence of glycerol, but its effectiveness is decreased by raising the pH to 8 and/or by adding glycerol
Co2+
-
maximal activity at 1 mM Co2+, strong decrease of activity above 4 mM
Co2+
-
5 mM, in presence of 5 mM Mg2+
Cu2+
Molinema dessetae
-
-
D-fructose
P0A3X6, -
10 mM, 19% inhibition
D-Fructose 1-phosphate
P0A3X6, -
10 mM, 26% inhibition
D-fructose 2,6-diphosphate
P0A3X6, -
0.3 mM, 35% inhibition
D-fructose 6-phosphate
A6YM33
99% residual activity at 2 mM
D-glucose 1-phosphate
A6YM33
95% residual activity at 2 mM
D-glucose 6-phosphate
A6YM33
93% residual activity at 2 mM
D-Phospholactate
-
-
diethyl dicarbonate
-
causes dissociation of the enzyme into dimers and monomers
DL-isocitrate
-
-
Fe2+
Molinema dessetae
-
-
-
fructose 1,6-diphosphate
-
-
fumarate
P0A3X6, -
10 mM, 31% inhibition
Glu
-
isoenzyme PEPC1 is more sensitive to inhibition than isoenzyme PEPC2
Glu
-
potent inhibitor at pH 7 in absence of glycerol, but its effectiveness is decreased by raising the pH to 8 and/or by adding glycerol
Glu
-
inhibition of enzyme form PEPC I and PEPC II, no inhibition of enzyme form PEPC III
glucose 6-phosphate
-
-
glutamate
-
IC50 of phospho-PEPC1: 2.1 mM, IC50 of dephospho-PEPC1: 2.2 mM; IC50 of phospho-PEPC2: 4.1 mM, IC50 of dephospho-PEPC2: 7.0 mM, enzyme form PEPC2
glycerol 3-phosphate
A6YM33
98% residual activity at 2 mM
GTP
-
10mM, 58% inhibition in presence of 5 mM Mg2+, 15% inhibition in presence of 15 mM Mg2+
guanidine hydrochloride
-
-
Hg2+
-
5 mM, in presence of 5 mM Mg2+
Isocitrate
Coccochloris peniocystis
-
-
KCl
-
0.05-1.0 M, 60% inhibition at 0.25 M, 27% inhibition at 0.1 M
L-Asp
-
2 mM, 95% decreases of activity of PEPC1 at pH 7.3, 49% decrease in activity of PEPC2 at pH 8
L-Asp
P0A3X6, -
more sensitive to inhibition by Asp at pH 9.0 than at pH 7.0
L-Asp
-, Q8XLE8
L-Asp competitively inhibits the enzyme with respect to the substrate, Mg2+-phosphoenolpyruvate
L-aspartate
-
10 mM, 41% inhibition in presence of 5 mM Mg2+ or 15 mM Mg2+
L-aspartate
A6YM33
98% residual activity at 2 mM
L-aspartate
-
-
L-aspartate
-
4 mM, complete inhibition
L-aspartate
Q97WG4, -
allosteric inhibitor
L-citrate
-
strong inhibition
-
L-Glu
-
2 mM, 96% decreases of activity of PEPC1 at pH 7.3, 22% decrease in activity of PEPC2 at pH 8
L-Malate
-
IC50: 3.84 mM for enzyme from mesocarop, stored in air, 5.95 mM for enzyme from mesocarop stored in 20% CO2, 2.01 mM for enzyme from peel stored in air
L-Malate
-
the inhibition by 0.16 mM L-malate, pH 7.3, decreases from 70 to 30%, along with a consistent increase in IC50 from 0.075 mM to 0.22 mM after 5 days of germination
L-Malate
-
inhibits wild-type enzyme
L-Malate
A6YM33
84% residual activity at 2 mM
L-Malate
Amaranthus edulis
-
-
L-Malate
-
weak inhibiton at physiological pH values
L-Malate
-
10 mM, 48% inhibition
L-Malate
Q97WG4, -
allosteric inhibitor
L-Phospholactate
-
-
lyso-phosphatidic acid
-
addition of 0.05 mM phosphatidic acid decreases PEPC activity to approximately 45% of the control activity
malate
-
competitive; L-malate
malate
Bryophyllum fedtschenkoi
-
-
malate
-
L-malate
malate
Bryophyllum fedtschenkoi
-
the day form of the enzyme is 10times more sensitive than the night form of the enzyme
malate
-
L-malate
malate
-
potent inhibitor at pH 7 in absence of glycerol, but its effectiveness is decreased by raising the pH to 8 and/or by adding glycerol
malate
-
competitive inhibitor of enzyme form PEPC I and enzyme form PEPC III, mixed-type inhibitor for enzyme form PEPC II
malate
-
reduction of the inhibitory effect by ethylene glycol and bicarbonate
malate
-
desensitization by bicarbonate
malate
-
the phosphorylated enzyme is less sensitive to malate
malate
-
2 mM, 96% decreases of activity of PEPC1 at pH 7.3, 59% decrease in activity of PEPC1 at pH 8
malate
-, Q9M3Y3
-
malate
-
feedback inhibitor
malate
-
IC50: 8 mM for PEPC activity in situ, 1.5 mM for PEPC activity in vitro
malate
-
IC50 of phospho-PEPC1: 0.075 mM, IC50 of dephospho-PEPC1: 0.029 mM; IC50 of phospho-PEPC2: 0.57 mM, IC50 of dephospho-PEPC2: 1.47 mM, enzyme form PEPC2
malate
-
dry heat, dark, 25C: 96% inhibition, 45C: 84% inhibition/dry heat, light, 25C: 59% inhibition, 45C: 31.2% inhibiton/wet heat, dark, 25C: 94%, 45C: 76% inhibition /wet heat, light, 25C: 46% inhibition, 45C: 17% inhibition
Maleate
Coccochloris peniocystis
-
-
-
Maleate
-
-
-
malonate
Bryophyllum fedtschenkoi
-
inhibits at pH 7.8, increases activity at pH 5.8
malonate
Coccochloris peniocystis
-
-
malonate
-, Q8XLE8
weak inhibitor
methyl phosphate
-
-
Mg-(1,2-epoxypropylphosphonic acid) complex
-
-
-
Mg2+
-
free, non-competitive. Substrate inhibition by Mg-phosphoenolpyruvate is caused by inhibition by high Mg2+ and ionic strength
microcystin-LR
-
PEPC2
Mn2+
-
maximal activity at 0.5 mM Mn2+, strong decrease of activity above 2 mM
Mn2+
-
substitution of 20 mM MnCl2 for 20 mM MgCl2 results in 90-100% inhibition
NaCl
-
200 mM, 50% inhibition
NaCl
-
0.05-1.0 M, 60% inhibition at 0.25 M, 27% inhibition at 0.1 M
oxaloacetate
-
-
oxaloacetate
-
-
oxaloacetate
-
-
oxaloacetate
Coccochloris peniocystis
-
-
oxaloacetate
-
-
p-hydroxymercuribenzoate
-
glutathione protects
PCMB
-
glutathione protects
PCMB
-
causes dissociation of the enzyme into dimers and monomers
phosphate
-
orthophosphate is noncompetitive with phosphoenolpyruvate
phosphate
Bryophyllum fedtschenkoi
-
-
phosphate
Coccochloris peniocystis
-
-
phosphate
-
activates at pH 7 in absence of glycerol, inhibits under other assay conditions
phosphate
-
-
phosphatidic acid
-
addition of 0.05 mM phosphatidic acid decreases PEPC activity to approximately 40% of the control activity. Inclusion of D-glucose 6-phosphate or L-malate do not change the effect of phosphatidic acid on PEPC, preincubation of the enzyme with 5 mM phosphoenolpyruvate prior to the addition of phosphatidic acid did not prevent inactivation either. The incubation of phosphatidic acid-inactivated PEPC with protein kinase A does not restore PEPC activity
phosphatidylinositol
-
addition of 0.05 mM phosphatidic acid decreases PEPC activity to approximately 40% of the control activity
phosphatidylinositol 4-phosphate
-
addition of 0.05 mM phosphatidic acid decreases PEPC activity to approximately 50% of the control activity
phosphatidylserine
-
addition of 0.05 mM phosphatidic acid decreases PEPC activity to approximately 80% of the control activity
phosphoenolpyruvate
-
above 1 mM
Phosphoglycolate
-
-
Picolinic acid
Coccochloris peniocystis
-
-
pyruvate
-
-
pyruvate
-
inhibition of enzyme form PEPC I and PEPC II, no inhibition of enzyme form PEPC III
Quinolinic acid
Coccochloris peniocystis
-
-
SO42-
Coccochloris peniocystis
-
-
Zn2+
-
substitution of 20 mM ZnCl2 for 20 mM MgCl2 results in 90-100% inhibition
Zn2+
-
5 mM, in presence of 5 mM Mg2+
Zn2+
Molinema dessetae
-
-
Mn2+
-
5 mM, in presence of 5 mM Mg2+, 72% inhibition
additional information
-
the enzyme is almost insensitive to feedback inhibition at neutral pH
-
additional information
-
not inhibited by phosphatidic acid, phosphatidylinositol, phosphatidylinositol 4-phosphate, lyso-phosphatidic acid, phosphatidylserine, phosphatidylcholine, and phosphatidylethanolamine
-
additional information
-
phosphatidylcholine and phosphatidylethanolamine have no effect on enzyme activity
-
additional information
-
the enzyme is poorly affected by L-Glu and L-Asp
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,2-Epoxypropylphosphonic acid
-
-
2-mercaptoethanol
-
activates
3-phosphoglycerate
P0A3X6, -
slight stimulation
3-Phosphoglyceric acid
-
activates
3-Phosphoglyceric acid
Coccochloris peniocystis
-
-
6-benzylaminopurine
-
natural cytokinin BAP
acetoacetyl-CoA
-
activates
acetyl-CoA
-
allosteric activator, PPC activity in extracts decreases by more than 75% in assays lacking acetyl-CoA
alpha-glycerophosphate
-
activates
Butyryl-CoA
-
activates
D-fructose 6-phosphate
-
2 mM, 1.2fold increase of activity of PEPC2 at pH 7.3, activity of PEPC2 at pH 8 is nearly identical to activity without glucose 6-phosphate
D-fructose 6-phosphate
-
-
D-glucose 1-phosphate
-
2 mM, 1.2fold increase of activity of PEPC2 at pH 7.3, activity of PEPC2 at pH 8 is nearly identical to activity without glucose 6-phosphate
D-glucose 6-phosphate
-
2 mM, 1.2fold increase of activity of PEPC2 at pH 7.3, activity of PEPC2 at pH 8 is nearly identical to activity without glucose 6-phosphate; 2 mM, 2fold increase of activity of PEPC1 at pH 7.3, 1.18fold increase in activity of PEPC1 at pH 8
D-glucose 6-phosphate
-
allosteric activator
D-glucose 6-phosphate
P04711
activates
D-glucose 6-phosphate
-
dry heat, dark, 25C: 253% activation, 45C: 347% activation/dry heat, light, 25C: 400% activation, 45C: 856% activation/wet heat, dark, 25C: 258% activation, 45C: 400% activation/wet heat, light, 25C: 456% activation, 45C: 908% activation
D-glucose 6-phosphate
-
-
D-glucose 6-phosphate
Q1XAT8
-
D-glucose 6-phosphate
Q1XAT9
-
D-glucose 6-phosphate
-, Q1XAT7
-
D-glucose 6-phosphate
-
-
D-glucose 6-phosphate
-
1.17fold activation of isoform Osppc4 at pH 7.3, 2.51fold activation of isoform Osppc2a at pH 7.3
D-glucose 6-phosphate
-
-
D-glucose 6-phosphate
-
-
dihydroxyacetone phosphate
-
activates
dihydroxyacetone phosphate
-
isoenzyme PEPC2 is inactivated 6fold by 2.0 mM, 52% activation by isoenzyme PEPC2
dihydroxyacetone phosphate
-
activates at pH 7 in absence of glycerol, but has no effect under other assay conditions
Dioxane
-
stimulates
ethanol
-
activates
fructose 1,6-bisphosphate
-
weak activation
fructose 1,6-bisphosphate
-
activates
fructose 1,6-bisphosphate
-
no effect
fructose 1,6-diphosphate
P0A3X6, -
activates
fructose 6-phosphate
Bryophyllum fedtschenkoi
-
activates at pH 7.8
fructose 6-phosphate
-
activates at pH 7 in absence of glycerol, but has no effect under other assay conditions
fructose 6-phosphate
-
2 mM, 2fold increase of activity of PEPC1 at pH 7.3, 1.27fold increase in activity of PEPC1 at pH 8
fructose diphosphate
-
activates
fusicoccin
-
rapid activation, reduces sensitivity towards the feedback-inhibitor malate
galactose 6-phosphate
Bryophyllum fedtschenkoi
-
activates at pH 7.8
Gln
P0A3X6, -
slight stimulation
Glu
P0A3X6, -
slight stimulation
glucose 1-phosphate
-
weak activation
glucose 1-phosphate
Bryophyllum fedtschenkoi
-
activates at pH 7.8
glucose 1-phosphate
-
activates at pH 7 in absence of glycerol, but has no effect under other assay conditions
glucose 1-phosphate
-
2 mM, 1.64fold increase of activity of PEPC1 at pH 7.3, 1.07fold increase in activity of PEPC1 at pH 8
glucose 1-phosphate
P0A3X6, -
slight stimulation
glucose 6-phosphate
-
significant activation
glucose 6-phosphate
-
maximal activation at 2 mM
glucose 6-phosphate
-
-
glucose 6-phosphate
-
activates
glucose 6-phosphate
-
-
glucose 6-phosphate
-
C4 plants and CAM plants
glucose 6-phosphate
-
no effect
glucose 6-phosphate
-
activates at pH 7 in absence of glycerol, but has no effect under other assay conditions
glucose 6-phosphate
-
activates
glucose 6-phosphate
-
desensitization by bicarbonate
glucose 6-phosphate
-
stimulates
glucose 6-phosphate
-
activates
glucose 6-phosphate
P0A3X6, -
slight stimulation
glucose 6-phosphate
-
activates wild-type enzyme
glucose 6-phosphate
-
-
glucose 6-phosphate
-
activates PEPC1
glutamine
-
activates
glutamine
-
isoenzyme PEPC1 is inactivated more than 4fold by 2 mM, 8% activation of isoenzyme PEPC2
Gly
-
significant activation
glycerol
-
activates
glycerol 3-phosphate
-
2 mM, 1.2fold increase of activity of PEPC2 at pH 7.3, activity of PEPC2 at pH 8 is nearly identical to activity without glucose 6-phosphate; 2 mM, 1.83fold increase of activity of PEPC1 at pH 7.3, 1.16fold increase in activity of PEPC1 at pH 8
glycine
-
allosteric activator
glycine
-
-
GTP
-
activates
Heptanoyl-CoA
-
activates
Hexanoyl-CoA
-
activates
His
-
stimulates
malate
-
2 mM, 1.2fold increase of activity of PEPC2 at pH 7.3, activity of PEPC2 at pH 8 is nearly identical to activity without glucose 6-phosphate
N-isopropoxycarbonyl-4-chlorophenylcarbamoyl-ethanolamine
-
synthetic preparation exhibiting cytokinin activity: kartolin-4
O-isopropyl-N-2-hydroxyethylcarbamate
-
synthetic preparation exhibiting cytokinin activity: kartolin-2
phosphate
-
dry heat, dark, 25C: 222% activation, 45C: 275% activation/dry heat, light, 25C: 321% activation, 45C: 636% activation/wet heat, dark, 25C: 225% activation, 45C: 315% activation/wet heat, light, 25C: 368% activation, 45C: 687% activation
phosphoenolpyruvate
-
free, allosteric activator
Polyethylene glycol
Bryophyllum fedtschenkoi
-
required for maximal activity
propionyl-CoA
-
absolute requirement for acetyl-CoA or propionyl-CoA
propionyl-CoA
-
activates
pyruvate
Coccochloris peniocystis
-
activates
succinyl-CoA
-
activates
thidiazuron
-
synthetic preparation exhibiting cytokinin activity: TDZ
Valeryl-CoA
-
activates
malonate
Bryophyllum fedtschenkoi
-
inhibits at pH 7.8, increases activity at pH 5.8
additional information
-
the results presented indicate that both the natural cytokinin BAP and synthetic preparations exhibiting cytokinin activity (TDZ, kartolin-2, and kartolin-4) attenuate the suppression PEPK activities in wheat seedlings and mature plant leaves, associated with water deficiency
-
additional information
-, Q8XLE8
not activated by D-glucose 6-phosphate
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.19
-
CO2
P00864
wild-type enzyme
0.04216
-
HCO3-
-
at pH 8.0 and 25C
0.1
-
HCO3-
P00864
wild type enzyme
0.11
-
HCO3-
-
-
0.17
-
HCO3-
-
-
0.23
-
HCO3-
-
pH 8.0, 25C, enzyme from roots grown in absence of Fe2+
0.24
-
HCO3-
-
pH 8.0, 25C, enzyme from roots grown in presence of Fe2+
0.25
-
HCO3-
-
enzyme form PEPC I
0.55
-
HCO3-
P00864
mutant enzyme Arg703Gly
0.7
-
HCO3-
-
enzyme form PEPC III
0.8
-
HCO3-
Coccochloris peniocystis
-
-
0.9
-
HCO3-
-
enzyme form PEPC II
1.28
-
HCO3-
-
isoenzyme PC-II
1.45
-
HCO3-
-
isoenzyme PC-I
1.6
-
HCO3-
Molinema dessetae
-
-
1.7
-
HCO3-
-
in presence of 0.04 mM acetyl-CoA
6.5
-
HCO3-
P00864
mutant enzyme Arg703Gly/Arg704Gly
0.05
-
phosphenolpyruvate
-
leaves are collected after 5 h into the dark, pH: 8.0; leaves are collected after 5 h into the light, pH: 8.0
-
0.06
-
phosphenolpyruvate
-
leaves are collected after 5 h in the dark, pH: 8.0; leaves are collected after 5 h in the light, pH: 8.0
-
0.09
-
phosphenolpyruvate
-
leaves are collected after 5 h into the light, pH: 8.0
-
0.1
-
phosphenolpyruvate
-
leaves are collected after 5 h into the light, pH: 8.0
-
0.1
-
phosphenolpyruvate
-
leaves are collected after 5 h into the dark, pH: 8.0
-
0.12
-
phosphenolpyruvate
-
leaves are collected after 5 h into the light, pH: 8.0
-
0.12
-
phosphenolpyruvate
-
leaves are collected after 5 h into the dark, pH: 8.0
-
0.17
-
phosphenolpyruvate
-
leaves are collected after 5 h into the dark, pH: 8.0
-
0.21
-
phosphenolpyruvate
Salsola richteri
-
leaves are collected after 5 h into the light, pH: 8.0
-
0.22
-
phosphenolpyruvate
Salsola richteri
-
leaves are collected after 5 h into the dark, pH: 8.0
-
0.038
-
phosphoenolpyruvate
-
at pH 8.0 and 25C
0.04
-
phosphoenolpyruvate
-
isoform Osppc2a, at pH 8.0 and 30C
0.047
-
phosphoenolpyruvate
-
isoenzyme PC-II
0.054
-
phosphoenolpyruvate
-
isozyme PPC1, at pH 8.5
0.06
-
phosphoenolpyruvate
-
pH 8.3
0.06
-
phosphoenolpyruvate
-
pH 8, PEPC1; pH 8, PEPC2
0.06
-
phosphoenolpyruvate
-, Q8XLE8
in the presence of 2 mM Mg2+, in 50 mM HEPES-NaOH buffer (pH 7.2), at 37C
0.065
-
phosphoenolpyruvate
-
extract from germinated seed
0.068
-
phosphoenolpyruvate
-
pH 7.8, enzyme from mesocarp, stored in 20% CO2
0.069
-
phosphoenolpyruvate
-
pH 8.0, 25C, enzyme from roots grown in presence of Fe2+
0.08
-
phosphoenolpyruvate
-
pH 8.4, 24C, pH 7.3, 24C, enzyme from cells grown in presence of phosphate or in absence of phosphate, assay in presence of glycerol
0.09
-
phosphoenolpyruvate
-
golden delicious, vascular bundle or seed
0.09
-
phosphoenolpyruvate
-
enzyme form PEPC I
0.09
-
phosphoenolpyruvate
-
desalted extracts from de-embryonated dry seed at pH 8
0.09
-
phosphoenolpyruvate
Q97WG4, -
pH 8.0, 80C
0.091
-
phosphoenolpyruvate
-
pH 8.0, 25C, enzyme from roots grown in absence of Fe2+
0.1
-
phosphoenolpyruvate
-
with Mn2+ as activator
0.1
-
phosphoenolpyruvate
-
isoenzyme PC-I
0.108
-
phosphoenolpyruvate
-
with Mg2+ as activator
0.12
-
phosphoenolpyruvate
-
pH 7.3, PEPC1; pH 7.3, PEPC2
0.12
-
phosphoenolpyruvate
-
pH 7.8, enzyme from mesocarp, stored in air
0.125
-
phosphoenolpyruvate
-
-
0.14
-
phosphoenolpyruvate
-
pH 7.3, no addition of phosphate, enzyme from light-adapted leaves
0.14
-
phosphoenolpyruvate
-
pH 7.8, enzyme from peel, stored in air
0.15
-
phosphoenolpyruvate
-
cox's orange Pippin, vascular bundle
0.15
-
phosphoenolpyruvate
-
enzyme form PEPC III
0.15
-
phosphoenolpyruvate
-
pH 7.3, 24C, pH 7.3, 24C, enzyme from cells grown in absence of phosphate, assay in presence of glycerol; pH 8.4, 24C, enzyme from cells grown in presence of phosphate, assay in absence of glycerol
0.16
-
phosphoenolpyruvate
-
pH 8.4, 24C, enzyme from cells grown in absence of phosphate, assay in absence of glycerol
0.16
-
phosphoenolpyruvate
-
isoform Osppc2a, at pH 7.3 and 30C
0.17
-
phosphoenolpyruvate
-
cox's orange Pippin, seeds
0.17
-
phosphoenolpyruvate
-
pH 7.3, 24C, pH 7.3, 24C, enzyme from cells grown in presence of phosphate, assay in presence of glycerol
0.18
-
phosphoenolpyruvate
-
enzyme form PEPC II
0.18
-
phosphoenolpyruvate
-
pH 7.3, addition of 30 mM phosphate, enzyme from light-adapted leaves
0.18
-
phosphoenolpyruvate
-
dephospho-PEPC2
0.18
-
phosphoenolpyruvate
-
phosphorylated isozyme PPC, at pH 7.3
0.19
-
phosphoenolpyruvate
P00864
wild-type enzyme; wild type enzyme, and mutant enzyme Arg703Gly/Arg704Gly
0.2
-
phosphoenolpyruvate
-
pH 8.2, enzyme from water stressed plants
0.21
-
phosphoenolpyruvate
-
-
0.21
-
phosphoenolpyruvate
-
-
0.23
-
phosphoenolpyruvate
-
pH 8.2
0.23
-
phosphoenolpyruvate
-
in presence of 0.04 mM acetyl-CoA
0.25
-
phosphoenolpyruvate
-
leaf
0.29
-
phosphoenolpyruvate
-
-
0.29
-
phosphoenolpyruvate
P00864
mutant enzyme Arg703Gly
0.29
-
phosphoenolpyruvate
-
stem
0.3
-
phosphoenolpyruvate
Bryophyllum fedtschenkoi
-
-
0.33
-
phosphoenolpyruvate
-
pH 7.3, no addition of phosphate, enzyme from dark-adapted leaves
0.34
-
phosphoenolpyruvate
-
dephosphorylated isozyme PPC1, at pH 7.3
0.35
-
phosphoenolpyruvate
-
pH 7
0.4
-
phosphoenolpyruvate
-
pH 7.3
0.41
-
phosphoenolpyruvate
-
pH 7.3, 24C, enzyme from cells grown in presence of phosphate, assay in absence of glycerol
0.42
-
phosphoenolpyruvate
-
pH 7.3, 24C, enzyme from cells grown in absence of phosphate, assay in absence of glycerol
0.44
-
phosphoenolpyruvate
-
-
0.46
-
phosphoenolpyruvate
-
-
0.49
-
phosphoenolpyruvate
-
-
0.49
-
phosphoenolpyruvate
-
pH 7.3, addition of 30 mM phosphate, enzyme from dark-adapted leaves
0.55
-
phosphoenolpyruvate
-
phosphoPEPC1; phospho-PEPC2
0.6
-
phosphoenolpyruvate
-
-
0.6
-
phosphoenolpyruvate
Coccochloris peniocystis
-
-
0.64
-
phosphoenolpyruvate
-
-
0.7
-
phosphoenolpyruvate
Bryophyllum fedtschenkoi
-
in absence of effectors, at 25C
0.74
-
phosphoenolpyruvate
-
-
0.79
-
phosphoenolpyruvate
-
C3 extract, light-harvested PEPC in the absence of D-glucose 6-phosphate
0.84
-
phosphoenolpyruvate
A6YM33
at pH 7.3
0.86
-
phosphoenolpyruvate
-
pH 7.2, enzyme from water stressed plants
0.87
-
phosphoenolpyruvate
A6YM33
at pH 8.0
0.92
-
phosphoenolpyruvate
-
dephosphoPEPC1
0.92
-
phosphoenolpyruvate
-
C3 extract, dark-harvested PEPC in the absence of D-glucose 6-phosphate
1.03
-
phosphoenolpyruvate
-
isoform Osppc4, at pH 8.0 and 30C
1.05
-
phosphoenolpyruvate
-
-
1.1
-
phosphoenolpyruvate
-
without activator
1.1
-
phosphoenolpyruvate
-
pH 8.0
1.25
-
phosphoenolpyruvate
-
pH 7.2
1.3
-
phosphoenolpyruvate
-
-
1.7
-
phosphoenolpyruvate
Bryophyllum fedtschenkoi
-
at 14C
1.89
-
phosphoenolpyruvate
-
C3 extract, light-harvested PEPC in the presence of 5 mM D-glucose 6-phosphate
2
-
phosphoenolpyruvate
-
isoform Osppc4, at pH 7.3 and 30C
2.26
-
phosphoenolpyruvate
-
C3 extract, dark-harvested PEPC in the presence of 5 mM D-glucose 6-phosphate
2.38
-
phosphoenolpyruvate
Molinema dessetae
-
-
2.4
-
phosphoenolpyruvate
Bryophyllum fedtschenkoi
-
at 40C
2.6
-
phosphoenolpyruvate
-
-
5
-
phosphoenolpyruvate
-
-
8.7
-
phosphoenolpyruvate
-
pH 7.0
7.6
-
HCO3-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
enzyme extract from plants after a 12 h dark period or a 12 h light period depending on pH
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
Sorghum sp.
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
Q1XAT8
K0.5 (phosphoenolpyruvate) (without 5 mM glucose 6-phosphate): 0.042 mM, K0.5 (phosphoenolpyruvate) (+ 5 mM glucose 6-phosphate): 0.025 mM
-
additional information
-
additional information
Q1XAT9
K0.5 (phosphoenolpyruvate) (without 5 mM glucose 6-phosphate): 0.157 mM, K0.5 (phosphoenolpyruvate) (+ 5 mM glucose 6-phosphate): 0.02 mM
-
additional information
-
additional information
-, Q1XAT7
K0.5 (phosphoenolpyruvate) (without 5 mM glucose 6-phosphate): 0.036 mM, K0.5 (phosphoenolpyruvate) (+ 5 mM glucose 6-phosphate): 0.013 mM
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.174
-
phosphoenolpyruvate
P15804
DELTAC4, deletion of the last 4 c-terminal amino acids
6.1
-
phosphoenolpyruvate
-, Q1XAT7
without 5 mM glucose 6-phosphate
7.2
-
phosphoenolpyruvate
P15804
G961V
9.5
-
phosphoenolpyruvate
P15804
DELTAC1, deletion of the last c-terminal amino acid
16
-
phosphoenolpyruvate
-, Q1XAT7
+ 5 mM glucose 6-phosphate
17.4
-
phosphoenolpyruvate
P15804
G961A
33
-
phosphoenolpyruvate
Q1XAT8
+ 5 mM D-glucose 6-phosphate; without 5 mM D-glucose 6-phosphate
38
-
phosphoenolpyruvate
Q1XAT9
+ 5 mM D-glucose 6-phosphate; without 5 mM D-glucose 6-phosphate
43
-
phosphoenolpyruvate
-
with Mn2+ as activator
66
-
phosphoenolpyruvate
P15804
-
69
-
phosphoenolpyruvate
-
with Mg2+ as activator
540
-
phosphoenolpyruvate
P00864
wild-type enzyme
additional information
-
additional information
P00864
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.13
-
(S)-malate
-
pH 7.3, no addition of phosphate, enzyme from dark-adapted leaves
0.21
-
(S)-malate
-
pH 7.3, no addition of phosphate, enzyme from light-adapted leaves
0.34
-
(S)-malate
-
pH 7.3, addition of 30 mM phosohate, enzyme from dark-adapted leaves
0.4
-
(S)-malate
-
pH 7.3, addition of 30 mM phosphate, enzyme from light-adapted leaves
0.025
-
Asp
P0A3X6, -
pH 9.0
2
-
Asp
P0A3X6, -
pH 7.5
0.2
-
L-Asp
-, Q8XLE8
in the presence of 2 mM Mg2+, in 50 mM HEPES-NaOH buffer (pH 7.2), at 37C
200
-
NaCl
-
-
additional information
-
additional information
-, Q9M3Y3
effect of ozone on Ki-value of malate
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.32
-
aspartate
-
IC50 of dephospho-PEPC1: 0.32 mM
0.35
-
aspartate
-
IC50 of phospho-PEPC1: 0.35 mM
2.6
-
aspartate
-
IC50 of phospho-PEPC2: 2.6 mM
4.5
-
aspartate
-
IC50 of dephospho-PEPC2: 4.5 mM, enzyme form PEPC2
2.1
-
glutamate
-
IC50 of phospho-PEPC1: 2.1 mM
2.2
-
glutamate
-
IC50 of dephospho-PEPC1: 2.2 mM
4.1
-
glutamate
-
IC50 of phospho-PEPC2: 4.1 mM
7
-
glutamate
-
IC50 of dephospho-PEPC2: 7.0 mM, enzyme form PEPC2
0.52
-
L-aspartate
-
dephosphorylated isozyme PPC1
1.14
-
L-aspartate
-
phosphorylated isozyme PPC1
33
-
L-aspartate
A6YM33
at pH 7.0
0.06
-
L-Malate
-
isoform Osppc2a, at pH 7.3 and 30C
0.07
-
L-Malate
-
leaf
0.075
-
L-Malate
-
the inhibition by 0.16 mM L-malate, pH 7.3, decreases from 70 to 30%, along with a consistent increase in IC50 from 0.075 mM to 0.22 mM after 5 days of germination
0.11
-
L-Malate
-
stem
0.2
-
L-Malate
-
-
0.23
-
L-Malate
-
samples are taken after 5 h into the dark, pH 7.2, 0.055 mM PEP
0.26
-
L-Malate
-
samples are taken after 5 h in the dark, pH 7.2, 0.1 mM PEP
0.3
-
L-Malate
-
dephosphorylated isozyme PPC1
0.33
-
L-Malate
-
samples are taken after 5 h in the dark, pH 7.2, 0.1 mM PEP
0.47
-
L-Malate
-
samples are taken after 5 h in the dark, pH 7.2, 0.1 mM PEP
0.6
-
L-Malate
-
samples are taken after 5 h into the light, pH 7.2, 0.055 mM PEP
0.68
-
L-Malate
-
phosphorylated isozyme PPC1
0.69
-
L-Malate
-
samples are taken after 5 h in the light, pH 7.2, 0.1 mM PEP
0.7
-
L-Malate
-
isoform Osppc4, at pH 7.3 and 30C
0.89
-
L-Malate
-
samples are taken after 5 h in the light, pH 7.2, 0.1 mM PEP
1.25
-
L-Malate
Salsola richteri
-
samples are taken after 5 h in the dark, pH 7.2, 0.1 mM PEP
1.91
-
L-Malate
-
samples are taken after 5 h in the light, pH 7.2, 0.1 mM PEP
2
-
L-Malate
-
samples are taken after 5 h into the dark, pH 7.2, 0.1 mM PEP
2.17
-
L-Malate
Salsola richteri
-
samples are taken after 5 h in the light, pH 7.2, 0.1 mM PEP
2.22
-
L-Malate
-
samples are taken after 5 h into the light, pH 7.2, 0.1 mM PEP
3.84
-
L-Malate
-
IC50: 3.84 mM for enzyme from mesocarop, stored in air, 5.95 mM for enzyme from mesocarop stored in 20% CO2, 2.01 mM for enzyme from peel stored in air
3.9
-
L-Malate
-
samples are taken after 5 h in the dark, pH 7.2, 0.1 mM PEP
3.93
-
L-Malate
-
samples are taken after 5 h in the light, pH 7.2, 0.1 mM PEP
11
-
L-Malate
A6YM33
at pH 7.0
0.029
-
malate
-
IC50 of dephospho-PEPC1: 0.029 mM
0.075
-
malate
-
IC50 of phospho-PEPC1: 0.075 mM
0.2
-
malate
-
harvest period: dark
0.4
-
malate
-
harvest period: light
0.57
-
malate
-
IC50 of phospho-PEPC2: 0.57 mM
1.47
-
malate
-
, IC50 of dephospho-PEPC2: 1.47 mM, enzyme form PEPC2
8
-
malate
-
IC50: 8 mM for PEPC activity in situ, 1.5 mM for PEPC activity in vitro
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.002
-
-
in a coupled assay with malate dehydrogenase
0.0047
-
-
lutescens 758, seedlings: after stress, 1 day, without treatment with O-isopropyl-N-2-hydroxyethylcarbamate
0.00521
-
-
lutescens 758, seedlings: after rehydration and after treatment with O-isopropyl-N-2-hydroxyethylcarbamate
0.00527
-
-
lutescens 758, seedlings: after rehydration and without treatment with O-isopropyl-N-2-hydroxyethylcarbamate
0.00536
-
-
lutescens 758, seedlings: after stress, 1 day, and after treatment with O-isopropyl-N-2-hydroxyethylcarbamate
0.00773
-
-
lutescens 758, seedlings: after treatment with O-isopropyl-N-2-hydroxyethylcarbamate
0.00883
-
-
lutescens 758, seedlings: without treatment with O-isopropyl-N-2-hydroxyethylcarbamate
0.01199
-
-
lutescens 758, leaves: after rehydration and without treatment with O-isopropyl-N-2-hydroxyethylcarbamate
0.012
-
-
photosynthetic rate: C3, harvest period: light, + 5 mM malate
0.01437
-
-
lutescens 758, leaves: after stress, 2 weeks, without treatment with O-isopropyl-N-2-hydroxyethylcarbamate
0.01518
-
-
Mironovskaya 808 leaves: stress, 1 day, and with N-isopropoxycarbonyl-O-4-chlorophenylcarbamoyl-ethanolamine treatment
0.01525
-
-
Mironovskaya 808 leaves: stress, 1 day, and with 6-benzylaminopurine treatment
0.0153
-
-
Mironovskaya 808 leaves: control (without any treatment)
0.01559
-
-
Mironovskaya 808 leaves: stress, 1 day, and without any treatment
0.016
-
-
photosynthetic rate: C3, harvest period: dark, + 5 mM malate
0.01601
-
-
Mironovskaya 808 leaves: stress, 1 day, and with tidiazuron
0.01819
-
-
lutescens 758, leaves: after stress, 2 weeks, and after treatment with O-isopropyl-N-2-hydroxyethylcarbamate
0.019
-
-
photosynthetic rate: C3, harvest period: light, + 5 mM malate and + 5 mM D-glucose 6-phosphate
0.01924
-
-
lutescens 758, leaves: after rehydration and after treatment with O-isopropyl-N-2-hydroxyethylcarbamate
0.02202
-
-
Mironovskaya 808 leaves: stress, 2 weeks, and without any treatment
0.023
-
-
Mironovskaya 808 leaves: stress, 1 day, and without any treatment
0.023
-
-
photosynthetic rate: C3, harvest period: light, control
0.02308
-
-
Mironovskaya 808 leaves: control (without any treatment)
0.02351
-
-
Mironovskaya 808 leaves: stress, 2 weeks, and with tidiazuron
0.02355
-
-
Mironovskaya 808 leaves: stress, 1 day, and with N-isopropoxycarbonyl-O-4-chlorophenylcarbamoyl-ethanolamine treatment
0.0236
-
-
Mironovskaya 808 leaves: stress, 2 weeks, and with 6-benzylaminopurine treatment
0.02366
-
-
Mironovskaya 808 leaves: rehydration, and without any treatment
0.0239
-
-
Mironovskaya 808 leaves: rehydration, and with tidiazuron
0.02403
-
-
Mironovskaya 808 leaves: stress, 2 weeks, and with N-isopropoxycarbonyl-O-4-chlorophenylcarbamoyl-ethanolamine treatment
0.02405
-
-
Mironovskaya 808 leaves: stress, 1 day, and with 6-benzylaminopurine treatment
0.0241
-
-
Mironovskaya 808 leaves: stress, 1 day, and with tidiazuron
0.02411
-
-
Mironovskaya 808 leaves: rehydration, and with 6-benzylaminopurine treatment
0.02422
-
-
Mironovskaya 808 leaves: rehydration, and with N-isopropoxycarbonyl-O-4-chlorophenylcarbamoyl-ethanolamine treatment
0.027
-
-
photosynthetic rate: C3, harvest period: dark, control
0.028
-
-
photosynthetic rate: C3, harvest period: dark, + 5 mM malate and + 5 mM D-glucose 6-phosphate
0.029
-
-
with 7.5 mM NH4Cl
0.03308
-
-
lutescens 758, leaves: without treatment with O-isopropyl-N-2-hydroxyethylcarbamate
0.03381
-
-
lutescens 758, leaves: after treatment with O-isopropyl-N-2-hydroxyethylcarbamate
0.034
-
-
clarified extract, at pH 8.5
0.036
-
-
isoenzyme PEPC1
0.04
-
-
with phosphate treatment, pH: 4.5, malate inhibition ratio: 0.68
0.0485
-
-
leaf, pH: 7.3
0.05
-
-
with phosphate treatment, pH: 5.0, malate inhibition ratio: 0.54
0.052
-
-
photosynthetic rate: C3, harvest period: light, + 5 mM D-glucose 6-phosphate
0.0626
-
-
stem, pH: 7.3
0.067
-
-
photosynthetic rate: C3, harvest period: dark, + 5 mM D-glucose 6-phosphate
0.0897
-
-
leaf, pH: 7.8
0.09
-
-
with phosphate treatment, pH: 4.0, malate inhibition ratio: 0.76
0.09
-
-
with phosphate treatment, pH: 4.0, malate inhibition ratio: 0.48
0.1
-
-
no phosphate treatment, pH: 5.0, malate inhibition ratio: 0.49; with phosphate treatment, pH: 5.0, malate inhibition ratio: 0.40
0.11
-
-
no phosphate treatment, pH: 4.0, malate inhibition ratio: 0.72
0.12
-
-
with phosphate treatment, pH: 4.5, malate inhibition ratio: 0.44
0.12
-
-
no phosphate treatment, pH: 4.5, malate inhibition ratio: 0.61
0.1245
-
-
stem, pH: 7.7
0.13
-
-
no phosphate treatment, pH: 4.0, malate inhibition ratio: 0.59
0.134
-
-
photosynthetic rate: C3, harvest period: dark, + 5 mM malate
0.137
-
-
-
0.138
-
-
isoenzyme PEPC2
0.15
-
-
no phosphate treatment, pH: 5.0, malate inhibition ratio: 0.65
0.16
-
-
no phosphate treatment, pH: 4.5, malate inhibition ratio: 0.69
0.17
-
-
photosynthetic rate: C4, harvest period: light, + 5 mM malate
0.213
-
-
photosynthetic rate: C3, harvest period: dark, control
0.23
0.26
Bryophyllum fedtschenkoi
-
-
0.3
-
A6YM33
clarified extract
0.326
-
-
photosynthetic rate: C4, harvest period: light, control
0.374
-
-
photosynthetic rate: C4, harvest period: light, + 5 mM malate and + 5 mM D-glucose 6-phosphate
0.433
-
-
photosynthetic rate: C4, harvest period: light, + 5 mM D-glucose 6-phosphate
0.449
-
-
photosynthetic rate: C3, harvest period: dark, + 5 mM malate and + 5 mM D-glucose 6-phosphate
0.461
-
-
photosynthetic rate: C3, harvest period: dark, + 5 mM D-glucose 6-phosphate
0.913
-
-
PEPC activity (micromol/mg chlorophyll/min) in Chinese common Japonica rice cultivar 9516 (female parent)
2.1
-
Q97WG4, -
pH 8.0, 80C
2.77
-
-
pH 8.0, 80C
4.4
-
-
with phosphate treatment, pH: 4.0, malate inhibition ratio: 0.54
5.2
-
-
-
5.32
-
-
with phosphate treatment, pH: 4.5, malate inhibition ratio: 0.49
5.8
-
-
with phosphate treatment, pH: 5.0, malate inhibition ratio: 0.43
8.46
-
-
no phosphate treatment, pH: 4.0, malate inhibition ratio: 0.33
8.87
-
Coccochloris peniocystis
-
-
9.15
-
-
no phosphate treatment, pH: 4.5, malate inhibition ratio: 0.24
9.51
-
-
no phosphate treatment, pH: 5.0, malate inhibition ratio: 0.58
11
-
-
dark-adapted enzyme form
13.52
-
-
PEPC activity (micromol/mg chlorophyll/min) in JAAS45 pure diploid lines (obtained by anther culture from F1 hybrids)
14.55
-
Molinema dessetae
-
-
15.78
-
-
PEPC activity (micromol/mg chlorophyll/min) in the forth generation of JAAS45
15.9
-
-
-
20.8
-
-
-
21
-
Bryophyllum fedtschenkoi
-
-
21
-
-
a light-adapted enzyme form
22.3
-
-
after 660fold purification, at pH 8.5
22.73
-
-
PEPC activity (micromol/mg chlorophyll/min) in PEPC transgenic rice germplasm (PC) (male parent)
23.58
-
-
-
24.2
-
-
PEPC1
25.2
-
A6YM33
after 152fold purification
26
-
Bryophyllum fedtschenkoi
-
-
28.5
-
-
-
29.2
-
-
PEPC2
29.4
-
-
-
37.2
-
-
-
42.3
-
-
-
51.09
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
evolution pattern of fatty acids and triacylglycerols contents is similar to that of PEPc activity, suggesting that PEPc may be involved in fatty acid and triacylglycerol biosynthesis during seed maturation; hybridol variety: PEPc activity does not exceed 5 micromol/h per gram of fresh weight during the first stages of maturation. It then highly increases to reach more than 30 micromol/h per gram of fresh weight; pactol variety: evolution of PEPc activity shows a classical curve, i.e. an increase during the most active phase of lipid accumulation in maturating seeds, followed by a rapid decrease until the end of seed maturation
additional information
-
P15804
the four C-terminal mutant enzymes display varying degrees of PEPC activity in vitro ranging from 23% of wild-type with the modest G961A substitution to only 0.2% for the DELTAC4-truncated form
additional information
-
-
iron deficiency responses are investigated in roots of soybean, disclosing a drastically reduced activity of the phosphoenolpyruvate carboxylase enzyme in soybean roots
additional information
-
-
the JAAS45 pollen line exhibits high levels of PEPC activity, manifesting higher saturated photosynthetic rates, photosynthetic apparent quantum yield (AQY), photochemical efficiency of photosystem II and photochemical and non-photochemical quenching, which indicate that the JAAS45 pollen line has a high tolerance to photo-inhibition/photooxidation under strong light and high temperature
additional information
-
-
PEPC activity of the Brachiaria hybrid (C4 plant) leaves is 51- to 129fold higher than that estimated for wheat and rice (both C3 plants). PEPC activity in leaves and roots of the Brachiaria hybrid increases up to two-and three-fold, respectively, and decreases the malate-inhibition ratio in leaves in response to P-deficiency
additional information
-
-
PEPC activity and malate-inhibition ratio are less affected in wheat and rice under P-deficiency
additional information
-
-
dry heat 25C, dark: 450 micromol/mg/chlorophyll/h, light: 944 micromol/mg/chlorophyll/h; dry heat 45C, dark: 705 micromol/mg/chlorophyll/h, light: 1834 micromol/mg/chlorophyll/h; effect of pretreatment 25C (dark, 30 min) + 25C (dark, 30 min): 238 micromol/mg/chlorophyll/h (none), 15.8 micromol/mg/chlorophyll/h (1 mM malate), 623 micromol/mg/chlorophyll/h (2 mM glucose-6-phosphate); effect of pretreatment 25C (dark, 30 min) + 25C (light, 30 min): 568 micromol/mg/chlorophyll/h (none), 231 micromol/mg/chlorophyll/h (1 mM malate), 2593 micromol/mg/chlorophyll/h (2 mM glucose-6-phosphate); effect of pretreatment 45C (dark, 30 min) + 25C (light, 30 min): 988 micromol/mg/chlorophyll/h (none), 636 micromol/mg/chlorophyll/h (1 mM malate), 8509 micromol/mg/chlorophyll/h (2 mM glucose-6-phosphate); wet heat 25C, dark: 448 micromol/mg/chlorophyll/h, light: 1069 micromol/mg/chlorophyll/h; wet heat 45C, dark: 836 micromol/mg/chlorophyll/h, light: 1942 micromol/mg/chlorophyll/h
additional information
-
-
relative to the female parent, the produced JAAS45 pollen lines exhibit high PEPC activity (17-fold increase) and also higher photosynthetic rates (about 36%-fold increase)
additional information
-
-
ozone is able to depress PEPc activity. As compared to chambered control atmosphere, significant declines in PEPc activity by circa 26% and 32% are recorded in + 60 and + 80 atmospheres, respectively
additional information
-
-
it is shown that there is a positive correlation between the activation and phosphorylation states of PEPC; light 2 h + 0.25 mM cycloheximide : 17% of maximal enzyme activity measured, phosphorylation status: 12% /dark 2 h + 0.25 mM cycloheximide : 14% of maximal enzyme activity measured, phosphorylation status: 7%; light 2 h + 10 mM DTT : 38% of maximal enzyme activity measured, phosphorylation status: 29% /dark 2 h + 10 mM DTT : 4% of maximal enzyme activity measured, phosphorylation status: 0%; light 2 h + 50 nM akadaic acid : 88% of maximal enzyme activity measured, phosphorylation status: 99% /dark 2 h + 50 nM okadaic acid : 48% of maximal enzyme activity measured, phosphorylation status: 60%; light 2 h : 71% of maximal enzyme activity measured, phosphorylation status: 100% /dark 2 h : 6% of maximal enzyme activity measured, phosphorylation status: 0%
additional information
-
Amaranthus edulis
-
PEPC activity is reduced to 42% and 3% of wild type activity in heterozygous and homozygous mutant plants, respectively
additional information
-
-
activity is peaking at midnight and then decreasing drastically until dawn
additional information
-
-
activity is peaking during the first 2 h of darkness and then decreasing drastically until dawn
additional information
-
Q5GM68, Q84VW9, Q8GVE8, Q9MAH0
highest activity is detected in roots, which shows expression of the four existing PEPC genes; highest activity is detected in roots, which shows expression of the four existing PEPC genes; highest activity is detected in roots, which shows expression of the four existing PEPC genes; highest activity is detected in roots, which shows expression of the four existing PEPC genes
additional information
-
O82072
higher PEPC activity in the developing grain than in flag leaf blade and glume during grain development. For 16 of the genotypes studied, the mean PEPC activity in the developing grain or glume at 15 and 25 days after flowering is significantly and positively correlated with final protein content of grain. Enzyme activities in glume and flag leaf blade are positively correlated with final grain weight but the activity in developing grain is weakly and negatively correlated with grain weight
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.3
-
-
tricine buffer
5.8
-
Bryophyllum fedtschenkoi
-
double optimum at pH 5.8 and pH 7.8
5.8
-
Molinema dessetae
-
-
7
9
-
p102kinase
7.3
-
-
assay at
7.4
-
-
Tris-HCl buffer
7.5
-
-
-
7.5
-
-
enzyme extract from plants after a 12 h dark period
7.5
-
-
assay at
7.5
-
-
-
7.6
-
-
in presence of both 1 mM malate and 5 mM glucose 6-phosphate
7.6
-
-
in situ PEPC activity
7.7
-
-
stem
7.8
-
Bryophyllum fedtschenkoi
-
double optimum at pH 5.8 and at pH 7.8
7.8
-
-
leaf
7.9
8.3
-
-
8
8.2
-
with or without 1 mM malate or 5 mM glucose 6-phosphate
8
8.5
A6YM33
-
8
-
-
double optimum at pH 8.0 and pH 8.4
8
-
Coccochloris peniocystis
-
-
8
-
-
enzyme extracts from plants after a 12 h light period
8
-
-
root-form PEPC and C4-form PEPC
8
-
-
PEPC2
8
-
-
activity of the enzyme from roots grown in absence of Fe2+ is about 4 times higher than the activity of the enzyme grown in presence of Fe2+
8
-
-
in vitro PEPC activity
8
-
-
assay at
8
-
P15804
assay at
8
-
-
assay at
8
-
Amaranthus edulis
-
assay at
8
-
-
assay at
8
-
Q1XAT8
assay at
8
-
Q1XAT9
assay at
8
-
-, Q1XAT7
assay at
8
-
-
Tris-H2SO4 buffer
8.1
-
-
-
8.2
-
-
assay at
8.4
-
-
double optimum at pH 8.4 and pH 8.0
8.5
-
-
PEPC1
8.5
-
-
assay at
8.6
-
-
at 30C
9
-
P0A3X6, -
at 30C
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.7
8
-
pH 5.7: about 65% of maximal activity, pH 8.0: about 50% of maximal activity
5.8
7.8
Bryophyllum fedtschenkoi
-
double optimum at pH 5.8 and at pH 7.8, minimum at pH 6.6
6.3
7.2
-
pH 6.3: 5% of maximal activity, pH 7.2: 92% of maximal activity
6.5
9
-
about 80% of maximal activity at pH 6.5 and at pH 9.0
6.5
9.5
-
pH 6.5: about 35% of maximal activity, pH 9.5: about 75% of maximal activity, PEPC2
7
7.6
-
pH 7.0: 55% of maximal activity, pH 7.6: optimum, in situ PEPC activity
7
8
-
pH 7.0: 90% of maximal activity of the root-form PEPC, 40% of maximal activity of the C4-form PEPC
7
9
-
50% of maximal activity at pH 7.0 and at pH 9.0
7
9.5
P0A3X6, -
pH 7.0: about 65% of maximal activity, pH 9.5: about 80% of maximal activity
7
9.5
-
pH 7.0: about 65% of maximal activity, pH 9.5: about 70% of maximal activity, Tris-H2SO4 buffer
7
9.6
-
pH 7.0: about 60% of maximal activity, pH 9.5: about 90% of maximal activity, PEPC1
7.3
8
-
pH 7.3: 50% of maximal activity, pH 8.0: optimum, in vitro PEPC activity
7.3
8.4
-
activity at pH 7.3 is almost 80% of the activity at pH 8.4
additional information
-
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
35
-
-
25
-
P15804
assay at
25
-
-
assay at
25
-
-
assay at
30
-
-
assay at
30
-
-
assay at
30
-
-
assay at
35
-
-
-
39
-
-
enzyme form PEPC I
40
-
-
isoenzyme PC-I
40
-
Coccochloris peniocystis
-
-
42
-
P0A3X6, -
at pH 7.5
43
-
-
enzyme form PEPC II and enzyme form PEPC III
67
-
-
activity increases from 20C to 67C
70
-
-
in presence of 0.3 M acetyl-CoA and 2 mM phosphoenolpyruvate
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
67
-
activity increases from 20C to 67C
30
50
P0A3X6, -
30C: about 40% of maximal activity, 50C: about 55% of maximal activity
50
80
-
about 50% of maximal activity at 50C and 80C
60
95
-
60C: about 30% of maximal activity, 95C: about 40% of maximal activity
70
95
-
70C: about 60% of maximal activity, 95C: about 55% of maximal activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.9
-
-
isoelectric focusing
6
-
-
Hvpepc3, Hvpepc4 and Hvpepc5
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
O82072
ear organ, protein content of grain as well as grain weight after flowering are studied in different winter wheat (Triticum aestivum L.) genotypes
Manually annotated by BRENDA team
-, O23946
PEPC1 and PEPC2 are expressed in fibres early in elongation but not in non-differentiating ovular epidermis
Manually annotated by BRENDA team
Rhodopseudomonas sp. No.7, Rhodopseudomonas sp. No. 7
-
grown photoanaerobically
-
Manually annotated by BRENDA team
Rhodopseudomonas sp. No.7, Rhodopseudomonas sp. No. 7
-
grown photoanaerobically
-
Manually annotated by BRENDA team
-
localized in most ovular and embryonic tissues. In early stages of seed development, enzyme protein is abundant in embryo and integuments, while at subsequent stages the enzyme accumulats in endosperm, nucellus and integuments. At late stages of seed development when both endosperm and nucellus are degraded, significant accumulation is observed in the embryo proper
Manually annotated by BRENDA team
-
on early stages of seed development, enzyme protein is abundant in embryo and integuments, while at subsequent stages the enzyme accumulats in endosperm, nucellus and integuments. At late stages of seed development when both endosperm and nucellus are degraded, significant accumulation is observed in the embryo proper
Manually annotated by BRENDA team
Q5GM68, Q84VW9, Q8GVE8, Q9MAH0
transcript detected; transcript detected in
Manually annotated by BRENDA team
Musa cavendishii
-
-
Manually annotated by BRENDA team
O82072
ear organ
Manually annotated by BRENDA team
-
discussion of the role of the enzyme in stomatal function
Manually annotated by BRENDA team
-
in early stages of seed development, enzyme protein is abundant in embryo and integuments, while at subsequent stages the enzyme accumulats in endosperm, nucellus and integuments
Manually annotated by BRENDA team
Bryophyllum fedtschenkoi
-
from young plants grown under controlled short-day conditions and an extraction buffer containing EDTA
Manually annotated by BRENDA team
-
in C4 plants, located in the mesophyll cells
Manually annotated by BRENDA team
-
dark-adapted and light adapted
Manually annotated by BRENDA team
-
the photosynthesis isoform Hvpepc4 is exclusively expressed in leaves during C4 induction
Manually annotated by BRENDA team
-
a significant decrease in PEPc protein expression is observed in the two highest ozone-enriched treatments + 60 atmosphere and + 80 atmosphere which reduces PEPc quantity by 31% and 41%, respectively
Manually annotated by BRENDA team
-
PEPC transcript expression rises to the peak at midnight and decreases to the minimum level at midday
Manually annotated by BRENDA team
-
PEPC transcript expression is peaking rapidly during the first 2 h of darkness and then decreasing drastically
Manually annotated by BRENDA team
Q1XAT8
weak expression detected by Northern blot-analysis
Manually annotated by BRENDA team
Q1XAT9
strong expression detected by Northern blot-analysis
Manually annotated by BRENDA team
-, Q1XAT7
weak expression detected by Northern blot-analysis
Manually annotated by BRENDA team
-
highest expression in the leaf blade
Manually annotated by BRENDA team
-
BTPC is present in leaf buds and young expanding leaves, but undetectable in fully expanded leaves
Manually annotated by BRENDA team
Amaranthus edulis
-
-
Manually annotated by BRENDA team
-
pre-climacteric fruit
Manually annotated by BRENDA team
-
immature
Manually annotated by BRENDA team
-
BTPC shows limited expression during pollen development
Manually annotated by BRENDA team
-
enzyme form PEPC III
Manually annotated by BRENDA team
-
of seedlings, roots show almost double the level of PEPC activity of shoots
Manually annotated by BRENDA team
Q5GM68, Q84VW9, Q8GVE8, Q9MAH0
only detected in; transcript detected; transcript detected in
Manually annotated by BRENDA team
-
2 enzyme form: PEPC I and PEPC II
Manually annotated by BRENDA team
-
developing. Localized in most ovular and embryonic tissues. In early stages of seed development, enzyme protein is abundant in embryo and integuments, while at subsequent stages the enzyme accumulats in endosperm, nucellus and integuments. At late stages of seed development when both endosperm and nucellus are degraded, significant accumulation is observed in the embryo proper
Manually annotated by BRENDA team
Amaranthus edulis
-
-
Manually annotated by BRENDA team
-
roots show almost double the level of PEPC activity of shoots
Manually annotated by BRENDA team
-
occurs at low levels in roots and cotyledons of germinated seeds
Manually annotated by BRENDA team
-
of seedlings, roots show almost double the level of PEPC activity of shoots
Manually annotated by BRENDA team
additional information
-
CrPpc1/2 polypeptide levels are up-regulated as the initial supply of NH4Cl decreases from 10 to 0.5 mM. However, within 5 h after re-supply of 10 mM NH4Cl to the N-deficient cells, the CrPpc1/2 levels reverts back nearly to those observed in high-N grown cells
Manually annotated by BRENDA team
additional information
-
phosphoenolpyruvate carboxylase contains two isoforms in Hydrilla verticillata, hvpepc3 and hvpepc4. Transcript expression of hvpepc4 is substantially up-regulated during C4 induction, especially in the light. It is suggested that hvpepc4 encodes the C4 photosynthetic PEPC, and hvpepc3 encodes an anaplerotic form
Manually annotated by BRENDA team
additional information
Q5GM68, Q84VW9, Q8GVE8, Q9MAH0
Atppc2 transcripts are found in all Arabidopsis organs suggesting that it is a housekeeping gene. Salt and drought exert a differential induction of PEPC gene expression in roots; salt and drought exert a differential induction of PEPC gene expression in roots; salt and drought exert a differential induction of PEPC gene expression in roots; salt and drought exert a differential induction of PEPC gene expression in roots. Atppc4 shows the highest induction in response to both stresses.
Manually annotated by BRENDA team
additional information
-
no expression in epidermis, vascular bundles, or guard cells
Manually annotated by BRENDA team
additional information
-
BTPC is abundant in the inner integument, cotyledon, and endosperm of developing seeds
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
BTPC localizes in vegetative cell cytoplasm
Manually annotated by BRENDA team
-
a BTPC/monoubiquitinated PTPC/PTPC complex is formed in the vegetative cell cytoplasm during late pollen development
Manually annotated by BRENDA team
-
transgenic rice plants C4-specific PEPC in cytosol
Manually annotated by BRENDA team
-
the enzyme partially localizes to membranes
Manually annotated by BRENDA team
-
mesophyll-cell
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
70680
-
-
predicted from cDNA
109700
-
Q5GM68, Q84VW9, Q8GVE8, Q9MAH0
deduced from cDNA
110000
-
P15804
SDS-PAGE
110000
-
-
SDS-PAGE
110200
-
Q5GM68, Q84VW9, Q8GVE8, Q9MAH0
deduced from cDNA
110300
-
Q5GM68, Q84VW9, Q8GVE8, Q9MAH0
deduced from cDNA
116600
-
Q5GM68, Q84VW9, Q8GVE8, Q9MAH0
deduced from cDNA
118000
-
A6YM33
PPC4, gel filtration
185300
-
-
gel filtration
200000
-
-
gel filtration
225700
-
-
sucrose density gradient centrifugation, isoenzyme PC-I
240000
-
-
gel filtration
260000
-
-
enzyme from darkened leaf extract, dimer, gel filtration
260000
-
-
gel filtration
270800
-
-
sucrose density gradient centrifugation, isoenzyme PC-II
280000
-
-
sucrose density gradient centrifugation
285000
-
-
enzyme from illuminated leaf extract, dimer, gel filtration
310000
-
Bryophyllum fedtschenkoi
-
gel filtration in presence of malate
340000
-
-
analytical ultracentrifugation
360000
-
-
gel filtration
361000
-
-
calculation from sedimentation and diffusion measurement
370000
-
Bryophyllum fedtschenkoi
-
gel filtration in absence of malate
380000
400000
-
gel filtration
389000
-
-
gel filtration
391000
-
-
PEPC1, gel filtration
400000
-
-
calculation from sedimentation velocity
400000
-
-
gel filtration
400000
-
-
low-molecular-mass isoenzyme PEPC1, gel filtration
400000
-
Crassula argentea
-
native PAGE
400000
-
-
gel filtration
400000
-
-
gel filtration
400000
-
-
non-denaturing PAGE
405000
-
-
gel filtration
410000
-
-
enzyme from darkened leaf extract, tetramer, gel filtration
410000
-
-
gel filtration, PEPC1
410000
-
-
class-1 PEPC, gel filtration
420000
-
-
enzyme from illuminated leaf extract, tetramer, gel filtration
430000
-
-
gel filtration
440000
-
-
gel filtration
450000
-
-
gel filtration
500000
-
Bryophyllum fedtschenkoi
-
gel filtration
560000
-
-
gel filtration
560000
-
Coccochloris peniocystis
-
gel filtration
570000
-
P0A3X6, -
gel filtration
650000
-
-
high-molecular-weight isoenzyme PEPC2, gel filtration
681000
-
-
gel filtration, PEPC2
900000
-
-
in late bicellular pollen of lily, BTPC forms a heterooctameric class-2 PEPC complex with PTPC of 900000 Da to express PEPC activity
910000
-
-
class-2 PEPC, gel filtration
984000
-
-
PEPC2, gel filtration
1186000
-
-
PEPC3, gel filtration
1590000
-
-
PEPC4, gel filtration
additional information
-
-
sequencing of the N-terminus, peptide mapping and immunological data suggest that the catalytic subunit of the enzyme is not related to the prokaryotic enzyme and is only distantly related to higher plant C4 and C3 enzymes
additional information
-
-
-
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
Bryophyllum fedtschenkoi
-
x * 105000
?
-
x * 97000, SDS-PAGE
?
-
x * 96000, SDS-PAGE
?
-
isoenzyme PEPC2 is a complex between the PEPC catalytic subunit of MW 100000 Da and other immunologically unrelated polypeptides of 50000-700000 Da
?
-
x * 109000, calculation from nucleotide sequence; x * 110000, SDS-PAGE
?
-
x * 43000, SDS-PAGE
?
Molinema dessetae
-
x * 64000, SDS-PAGE in presence of 2-mercaptoethanol
?
-
x * 110000, SDS-PAGE
?
-
x * 104000, SDS-PAGE
?
-
1 * 12500 + 6 * 60600 + 2 * 16600 + 2 * 10300, PEPC2, SDS-PAGE
?
-
x * 118000, BTPC, SDS-PAGE
?
Q97WG4, -
x * 58772, calculated from sequence
?
Chlamydomonas reinhardtii CW-15 cc1883
-
isoenzyme PEPC2 is a complex between the PEPC catalytic subunit of MW 100000 Da and other immunologically unrelated polypeptides of 50000-700000 Da
-
?
-
x * 58772, calculated from sequence
-
dimer
Crassula argentea
-
the enzyme exists as tetramer during the night and as a dimer during the day
heteromer
-
x * 669000, class-2 PEPC enzyme-forms a high-molecular-mass, hetero-oligomeric complex containing both CrPpc1 (p109) and CrPpc2 (p131) polypeptides. Determined by: 1D nativePAGE and 2D BN/SDSPAGE, combined with immunoblotting
heterooctamer
-
4 * 107000 + 4 * 118000, class-2 PEPC, SDS-PAGE
heterooctamer
-
in late bicellular pollen of lily, BTPC forms a heterooctameric class-2 PEPC complex with PTPC to express PEPC activity
homotetramer
-
4 * 102000, isoform PEPC1, SDS-PAGE
homotetramer
-
4 * 107000
homotetramer
-
4 * 111000 Determined by: 1D native-PAGE and 2D BN-/SDS-PAGE, combined with immunoblotting
homotetramer
-
4 * 107000, native enzyme, gel filtration
homotetramer
P27154
4 * 105000, nondenaturing PAGE
homotetramer
-
4 * 107000, class-1 PEPC, SDS-PAGE
homotetramer
-
4 * 107000, PTPC, SDS-PAGE
homotetramer
-
4 * 60000, SDS-PAGE
octamer
-
4 * 107000 + 4 * 64000, PEPC2, SDS-PAGE
octamer
-
x * 107000 + x * 64000, enzyme form PEPC2
tetramer
-
4 * 93000, SDS-PAGE
tetramer
-
4 * 130000, SDS-PAGE
tetramer
Bryophyllum fedtschenkoi
-
4 * 105000, SDS-PAGE
tetramer
-
4 * 50000, SDS-PAGE
tetramer
-
4 * 100000, SDS-PAGE
tetramer
Bryophyllum fedtschenkoi
-
4 * 112000, SDS-PAGE
tetramer
Crassula argentea
-
the enzyme exists as tetramer during the night and as a dimer during the day
tetramer
-
-
tetramer
-
4 * 60000, SDS-PAGE
tetramer
-
4 * 100000, isoenzyme PEPC1, SDS-PAGE
tetramer
-
4 * 110000, SDS-PAGE
tetramer
Crassula argentea
-
4 * 100000, SDS-PAGE
tetramer
-
4 * 100000, SDS-PAGE
tetramer
-
4 * 95000, SDS-PAGE
tetramer
-
4 * 102000, SDS-PAGE
tetramer
-
4 * 88000, SDS-PAGE
tetramer
-
4 * 100000, SDS-PAGE
tetramer
-
2 * 19900 + 3 * 27900 + 5 * 30600 + 4 * 21600, PEPC3, SDS-PAGE; 3 * 22100 + 2 * 14900 + 7 * 30900 + 8 * 32100, PEPC4, SDS-PAGE; 4 * 102000, PEPC1, SDS-PAGE
tetramer
-
4 * 107000, PEPC1, SDS-PAGE
tetramer
P0A3X6, -
4 * 120000, SDS-PAGE
tetramer
-
-
tetramer
-, Q8XLE8
X-ray crystallography, analytical ultracentrifugation, or sedimentation velocity analysis
tetramer
Chlamydomonas reinhardtii CW-15 cc1883
-
4 * 100000, isoenzyme PEPC1, SDS-PAGE
-
tetramer
Rhodopseudomonas sp. No.7, Rhodopseudomonas sp. No. 7
-
4 * 102000, SDS-PAGE
-
homotetramer
-
4 * 60000, SDS-PAGE
-
additional information
Crassula argentea
-
dilution induces a dissociation of the native tetramer to a less active dimer, preincubation of the dilute enzyme with phosphoenolpyruvate stabilizes the tetramer while the presence of malate induces dimer formation, glucose 6-phosphate induces tetramer formation of the dilute enzyme, both the substrate phosphoenolpyruvate and the activator glucose 6-phosphate stabilize the active tetramer via binding and interaction at an activator site separate from the active site
additional information
-
concentration-dependent dissociation of tetrameric into dimeric forms
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phosphoprotein
-
a marked diurnal rhythm can be seen in the PEPC protein levels and phosphorylation status during May (summer month). In contrast, only the phosphorylation status increases during the day in December (winter month)
phosphoprotein
-
PEPC is phosphorylated only during the dark period, especially at midnight
phosphoprotein
-
purified PPC1 is phosphorylated at Ser-11, in vivo phosphorylation of isoform PPC1 during phosphate stress also activates this enzyme at pH 7.3 by significantly lowering its Km(phosphoenolpyruvate) value and sensitivity to inhibition by L-malate and L-Asp, while increasing its activation by D-glucose-6-phosphate
phosphoprotein
-
the phosphoenolpyruvate carboxylase kinase gene product PPCk1 is responsible for leaf PEPC phosphorylation
phosphoprotein
-
class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
-
the enzyme may exist in a dephosphorylated form in cell grown in absence of phosphate and in cells grown in presence of phosphate
phosphoprotein
-
class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
-
-
phosphoprotein
-
PEPC is phosphorylated only during the dark period, especially during the first 2 h of darkness
phosphoprotein
-
class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
-
the protein phosphatase inhibitor, okadaic acid, promotes the phosphorylation of PEPCK
phosphoprotein
Musa cavendishii
-
class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
P27154
-
phosphoprotein
-
class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
-
Ser6 is phosphorylated. Ser6 phosphorylation of the p107 subunit increases KM-value of PEPC2 for phosphoenolpyruvate and sensitivity to L-malate, glutamic acid, and aspartic acid inhibition. Phosphorylation of subunit p107 is promoted during development of Ricinus communis but disappears during desiccation. The p107 stage VII becomes fully dephosphorylated in plants 48 h following excision of Ricinus communis pods or following 72 h of dark treatment of intact plants; Ser6 is phosphorylated. Ser6 phosphorylation of the p107 subunit increases PEPC1 activity at pH 7.3 by decreasing its KM for phosphoenolpyruvate and sensitivity to L-malate inhibition, while enhancing glucose 6-phosphate activation
phosphoprotein
-
phosphorylation at Ser425 is promoted during seed development, Ser425 phosphorylation results in significant bacterial-type phosphoenolpyruvate carboxylase inhibition
phosphoprotein
-
class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
-
PTPC of castor oil seeds is activated by phosphorylation at Ser-11 during endosperm development
ubiquitination
-
PTPC of castor oil seeds is inhibited by monoubiquitination at Lys-628 during germination
phosphoprotein
-
class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
-
C4-PEPC is regulated by phosphorylation by a phosphoenolpyruvate carboxylase kinase, n-butanol leads to the partial inhibition of the C4-PEPC phosphorylation
phosphoprotein
-
-
phosphoprotein
-
class-1 PEPC phosphorylation uniformly results in enzyme activation at physiological pH
phosphoprotein
-
the guard cell enzyme is regulated by reversible phosphorylation of at least one isoform
phosphoprotein
Amaranthus edulis
-
PEPC proteins are phosphorylated in dry seeds, and PEPC phosphorylation does not occur in vivo during seed imbibition in the presence of 32P-phosphate
additional information
-
modulation of phosphoenolpyruvate carboxylase in vivo by Ca2+, possible involvement of Ca2+ in up-regulation of PEPC-protein kinase
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging drop vapor diffusion method, using 1.25-1.5 M sodium malonate, pH 7.0, as precipitant
-, Q8XLE8
PEPC complexed with L-Asp, at 2.8 A resolution; three-dimensional structure of the enzyme complexed with the allosteric inhibitor L-Asp, determined by X-ray diffraction at 2.8 A resolution
P00864
sitting drop vapor diffusion method, crystal structure of the enzyme complexed with Mn2+, the phosphoenolpyruvate analog 3,3-dichloro-2-dihydroxyphosphinoylmethyl-2-prepenoate and an allosteric inhibitor, aspartate, determined at 2.35 A resolution
P00864
hanging-drop vapour-diffusion method with PEG 8000 as precipitant at pH 7.5. the crystals belong to space group C222(1), with unit-cell dimensions a = 160.2, b = 175.6, c = 255.5 A, and diffract to 3.2 A resolution
-
sitting drop vapor diffusion method, crystal structure determined at 3.0 A resolution
P04711
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
8.5
-
PEPC activity at pH 7.0 is approximately 50% of that occurring at pH 8.5
7
-
-
15C, in presence of 1 mM dithiothreitol
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
-2
-
-
activity increases after exposition of fruits to -2C for 4 h
0
-
-
45 min, 70% loss of activity without addition of stabilizing agent, 14% loss of activity in presence of 10 mM MgCl2, 8% loss of activity in presence of 4 mM phosphoenolpyruvate, 73% loss of activity in presence of 5 mM pyruvate, 41% loss of activity in presence of 6 mM L-malate, 5% loss of activity in presence of 10 mM glucose-6-phosphate
15
-
-
pH 7.0, in presence of 1 mM dithiothreitol
24
-
-
45 min, 12% loss of activity without addition of stabilizing agent, 1% loss of activity in presence of 10 mM MgCl2, no loss of activity in presence of 4 mM phosphoenolpyruvate, 17% loss of activity in presence of 5 mM pyruvate, no loss of activity in presence of 6 mM L-malate, no loss of activity in presence of 10 mM glucose-6-phosphate
25
-
-
30 min, pH 7, no loss of activity
30
-
-
30 min, pH 7, 15% loss of activity
30
-
-
3 min, no loss of activity, PEPC1
35
-
-
instable above
35
-
-
30 min, 40% loss of activity
35
-
-
3 min, 19% loss of activity, PEPC1
40
-
-
30 min, pH 7, 89% loss of activity
40
-
-
3 min, 25% loss of activity, PEPC1
45
-
-
50% inactivation after 87 s, isoenzyme PC-I. 50% inactivation after 100 s, isoenzyme PC-II
45
-
-
2 min, 56% loss of activity
45
-
-
rapid decrease of activity above
45
-
-
30 min, pH 7, complete loss of activity
45
-
-
3 min, 40% loss of activity, PEPC1; 3 min, no loss of activity, PEPC2
50
-
-
50% inactivation after 18 s, isoenzyme PC-I. 50% inactivation after 28 s, isoenzyme PC-II
50
-
Bryophyllum fedtschenkoi
-
10 min, only small activity loss below 50C
50
-
-
enzyme form PEPC I: complete inactivation after 15 s, enzyme forms PEPC II and PEPC III: complete inactivation after 25 s
50
-
-
3 min, 20% loss of activity, PEPC2; 3 min, 82% loss of activity, PEPC1
50
-
P0A3X6, -
60 min, stable
55
57
Bryophyllum fedtschenkoi
-
10 min, 50% denaturation
55
-
-
50% inactivation after 13 s, isoenzyme PC-I. 50% inactivation after 17 s, isoenzyme PC-II
55
-
-
3 min, complete loss of activity, PEPC1; 3 min, complete loss of activity, PEPC2
60
65
-
rapid inactivation
60
-
-
2 min, complete loss of activity
60
-
P0A3X6, -
10 min, 50% loss of activity
67
-
-
10 min, inactivation
70
-
P0A3X6, -
20 min, complete inactivation
75
-
-
3 min, inactivation
75
-
-
2 h, no loss of activity
80
-
-
50% loss of activity after 240 min
80
-
-
2 h, no loss of activity
85
-
-
half-life: 85 min
90
-
-
50% loss of activity after 20 min
90
-
-
half-life: 110 min
90
-
-
60 min, 50% loss of activity
95
-
-
half-life: 50 min
95
-
-
10 min, 50% loss of activity
100
-
-
50% loss of activity after 1 min
100
-
-
1 min, 50% loss of activity
additional information
-
Bryophyllum fedtschenkoi
-
reversible loss of activity between 30C and 45C, may represent a temperature-dependent equilibrium between two forms of enzyme
additional information
-
-
malate, 10 mM, protects from inactivation at 55C, at pH 5.5, but not at pH 8.3; phosphoenolpyruvate, 5 mM, stabilizes the enzyme at 37C in plant extract
additional information
-
-
10 mM Mg2+ stabilizes the enzyme against cold inactivation. At low Mg2+ concentrations, 4 mM, the enzyme is strongly protected by phosphoenolpyruvate, glucose-6-phosphate, and, partially, by L-malate
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
glycerol increases stability
-
10 mM Mg2+ stabilizes the enzyme against cold inactivation. At low Mg2+ concentrations, 4 mM, the enzyme is strongly protected by phosphoenolpyruvate, glucose-6-phosphate, and, partially, by L-malate
-
thiol protecting agents stabilize during purification
Bryophyllum fedtschenkoi
-
malate, 10 mM, protects from inactivation at 55C, at pH 5.5, but not at pH 8.3
-
phosphoenolpyruvate, 5 mM, stabilizes the enzyme at 37C in plant extract
-
malate, 10 mM, protects from inactivation at 55C, at pH 5.5, but not at pH 8.3
-
phosphoenolpyruvate, 5 mM, stabilizes the enzyme at 37C in plant extract
-
malate, 10 mM, protects from inactivation at 55C, at pH 5.5, but not at pH 8.3
Panicum schenckii
-
phosphoenolpyruvate, 5 mM, stabilizes the enzyme at 37C in plant extract
Panicum schenckii
-
desalted enzyme, in Tris buffer, pH 7.5, room temperature, half-life is 3-4 h
-
malate, 10 mM, protects from inactivation at 55C, at pH 5.5, but not at pH 8.3
-
phosphoenolpyruvate, 5 mM, stabilizes the enzyme at 37C in plant extract
-
malate, 10 mM, protects from inactivation at 55C, at pH 5.5, but not at pH 8.3
-
phosphoenolpyruvate, 5 mM, stabilizes the enzyme at 37C in plant extract
-
retains full activity after exposure to 0.5 M guanidine-HCl at 30C for 20 h
P0A3X6, -
inactivated by trypsin under non-catalytic conditions, resulting in a truncated enzyme having molecular mass of about 80000 Da. In presence of substrate very little inactivation is observed although the subunit molecular mass is reduced to 90000 Da
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-4C or -20C, marked decrease in activity after 2 months
-
in liquid N2 in presence of 50% v/v glycerol, up to 3 months the enzyme largely retains its full activity
-
4C, in (NH4)2SO4 suspension, 1 month stable
Bryophyllum fedtschenkoi
-
0-4C, stable for 3 d
-
-80C, concentrated, undesalted solution containing 33% v/v glycerol, stable for at least 6 weeks
Coccochloris peniocystis
-
-14C, isoenzyme I loses 50% of its activity in presence of ethanol
-
-16C, 10% glycerol, 1% bovine serum albumin, stable for up to 1 year
-
-80C, stable for at least 1 month
-
-12C, 0.4 M potassium phosphate buffer containing 0.5 M glucose, 1 mM EDTA, 1 mM MgCl2, no loss of activity after 3 months
-
-20C, little loss of activity after 8 months
-
-20C, 50% (v/v) glycerol, the final PPC4 preparation proves difficult to store as it slowly loses activity and is completely inactivated when rapidly thawed after freezing in liquid N2
A6YM33
4C, in 50% ammonium sulfate, stable for 2-3 weeks
-
-20C, 0.04 M Tris/HCl buffer, pH 7.8, 2.0 mM dithiothreitol, 2.0 mM MgCl2, 1.0 mM EDTA, 20% glycerol, 1.0 mM Pro, stable for at least 4 weeks
-
-18C, 10 mM 2-mercaptoethanol, stable for several weeks
-
-18C, 20% sucrose solution, stable for 14 days
-
-20C, stable for several weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ammonium sulfate precipitation, butyl-Sepharose column chromatography, Fractogel EMD DEAE-650 colum chromatography, Mono Q column chromatography, and Superdex-200 gel filtration
-
-
Bryophyllum fedtschenkoi
-
2 forms: a night form and a day form
Bryophyllum fedtschenkoi
-
a high-molecular-mass isoform, PEPC2, and a low-molecular-mass isoform, PEPC1
-
isoform-specific purification of CrPpc1 and CrPpc2 is carried out by affinity-purification of using CrPpc1 and CrPpc2 peptide antibodies
-
recombinant His-tagged Ppc1, expression in Escherichia coli; recombinant His-tagged Ppc2, expression in Escherichia coli
P81831, Q6R2V6
Sephadex G-25 gel filtration
-
affinity chromatography and gel filtration
-, Q8XLE8
-
Coccochloris peniocystis
-
large scale purification
-
partial, 2 isoenzymes: I and II
-
partial
-
partial
-
partial
-
-
Molinema dessetae
-
partial, 2 isoforms: PEPC1 and PEPC2
-
butyl-Sepharose column chromatography
-
Ni-NTA column chromatography, Superose-6 gel filtration, and Superdex 200 gel filtration
A6YM33
Ni2+ affinity resin column chromatography, Superdex-200 gel filtration, and Superose-6 gel filtration
-
affinity purification
P15804
recombinant enzyme
-
wild type and mutant enzymes S8C, and S8D
Sorghum sp.
-
partial
-
a dark-adapted enzyme form and a light-adapted enzyme form
-
isoenzyme PC-I and PC-II
-
recombinant
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli
Q1XAT8
expressed in Escherichia coli
Q1XAT9
expressed in Escherichia coli
-, Q1XAT7
expressed in Escherichia coli with an N-terminal His-tag; expressed in Escherichia coli with an N-terminal His-tag; expressed in Escherichia coli with an N-terminal His-tag; expressed in Escherichia coli with an N-terminal His-tag
Q5GM68, Q84VW9, Q8GVE8, Q9MAH0
expressed in Sinorhizobium meliloti mutant RmF991
-
cloning of ppc1 in Escherichia coli; cloning of ppc2 in Escherichia coli
P81831, Q6R2V6
expressed in Escherichia coli
-, Q8XLE8
cloned in Escherichia coli DH5alpha. Knock-out as well as over-expression mutants are constructed and characterized. Knocking out phosphoenolpyruvate carboxylase decreases the maximum cell density by 14% and increases the acetate excretion by 7%. Over-expression of phosphoenolpyruvate carboxylase increases the maximum cell dry weight by 91%. No acetate excretion is detected at these increased cell densities
-
expression in Escherichia coli
-
using the antisense technique the expression of Ljpepc1 is decreased in three independent transgenic Lotus japonicus plants (designated as Asppc1, Asppc2 and Asppc3). In nodules of Asppc plants, PEPC activity is reduced to about 10% of that of non-transformants and the plants show typical nitrogen-deficient symptoms without a supply of nitrogen nutrient, and returned to normal growth when nitrate was supplied at 2.5 mM. The acetylene reduction activity per fresh weight of nodules of these Asppc plants decreases by 29% at 35 days after infection
-
expression in Escherichia coli
-
carbon metabolism is analysed in generated transgenic rice plants expressing either PEPC or both phosphoenolpyruvate carboxykinase (PCK) and PEPC: Results suggest that overexpression of PEPC enhances the anaplerotic pathway rather than the initial carbon fixation of the C4-like photosynthetic pathway, and that elevated PEPC activity in combination with PCK activity contributes little to C4-like carbon flow
-
to elucidate the photosynthetic physiological characteristics and the physiological inherited traits of rice hybrids and their parents, physiological indices of photosynthetic CO2 exchange and chlorophyll fluorescence parameters are measured in leaves of the maize phosphoenolpyruvate carboxylase (PEPC) transgenic rice as the male parent, sp. japonica rice cv. 9516 as the female parent, and the stable JAAS45 pollen line. The results reveal that the PEPC gene can be stably inherited and transferred from the male parent to the JAAS45 pollen line
-
high level of PEPC gene is stably inherited and transferred from the male parent, PEPC transgenic rice, into a female parent, japonica rice cv. 9516. The produced JAAS45 pollen lines are more tolerant to photoinhibition and to photo-oxidative stress.
-
expressed in Escherichia coli BL21(DE3) cells
A6YM33
expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL cells
-
cloned as a Histag-fusion protein in an Escherichia coli PEPC- (Ppc-) strain
P15804
expression in Escherichia coli
-
phosphoenolpyruvate carboxylase and Lactococcus lactis pyruvate carboxylase are overexpressed in Escherichia coli concurrently to improve the production of succinate. This coexpression system is also applied to mutant strains of Escherichia coli strategically designed by inactivating the competing pathways of succinate formation. Coexpression of phosphoenolpyruvate carboxylase and Lactococcus lactis pyruvate carboxylase is effective in depleting pyruvate accumulation and increasing the production of metabolites
-
subcloned into the streptomycete high-copy-number plasmid vector pIJ486 and transferred into Streptomyces lividans
-
expression in Escherichia coli as a fusion with the Escherichia coli maltose-binding protein
Q97WG4, -
expressed in Arabidopsis thaliana under the control of the cauliflower mosaic virus 35S promoter. SvPEPC is capable of efficiently exerting its activity in the plant cell environment so as to cause imbalance between aromatic and non-aromatic amino acid synthesis
-
expression in Escherichia coli
P0A3X6, -
expression in Escherichia coli
-
phosphoenolpyruvate carboxylase is ectopically overexpressed in Vicia narbonensis seeds: Transgenic embryos take up more carbon and nitrogen. Changes in dry to FW ratio, seed fill duration and major seed components indicate altered seed development. Array-based gene expression analysis of embryos reveals upregulation of seed metabolism, especially during the transition phase and at late maturation.
-
expression in Escherichia coli as a fusion protein, the extra 159 amino acid residues fused at the N-terminus of the enzyme protein have no effect on catalytic and regulatory properties
-
expression in Escherichia coli BL21(DE3)pLysS
-
isozymic forms are encoded by a small gene family
-
root enzyme
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
when examined at 06.00 h and 15.00 h during different months of the year, the activity of PEPC is maximal in summer (e.g. May) and minimal in winter (e.g. December). The maximum activity of PEPC is at 15.00 h during a typical day in all months
-
BTPC expression initiates after the last mitosis before pollen germination
-
PEPC activity is 3times higher in virus-infected (PVYNTN) plant leaves compared to healthy plants
P27154
PEPC is up-regulated during infection of Nicotiana tabacum plants by the potato virus
-
Spartina densiflora individuals from Patagonia have 60% higher PEPC specific activity than plants from Brazil, Argentina and the Iberian Peninsula due to higher levels of PEPC protein that coincide with lower activation mediated by phosphorylation. The high PEPC protein levels of the Patagonian ecotype are a response to lower light activation level of the enzyme, as judged by the low PEPC phosphorylation state
-
PEPC levels increase as the grains progress up to mid ripening stage (14 and 21 days after anthesis for bolder and smaller grains respectively) followed by a gradual decrease towards maturity
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
R438C
P00864
Arg438Cys has an increased tendency to dissociate into dimers. Mutant enzyme Arg703Gly shows a 5fold decreased turnover number compared to the wild type enzyme
delataC1
P15804
deletion of the last c-terminal amino acid. kcat: 9.5/sec (phosphoenolpyruvate),12.6% of wild type catalytic activity
delataC4
P15804
deletion of the last 4 c-terminal amino acids. kcat: 0.174/sec (phosphoenolpyruvate), 0.14% wild type catalytic activity
G961A
P15804
kcat: 17.4/sec (phosphoenolpyruvate), 24.3% of wild type catalytic activity
S8C
Sorghum sp.
-
he S-carboxymethylated S8C mutant enzyme, in contrast to the SH-modified wild type protein, has an increased I0.5 value for L-malate similar to that of the phosphorylated Ser8 enzyme and the S8D mutant protein
D228N
-
reduced apparent affinity for the activator glycine
E229A
-
maximal activation caused by glycine is greatly reduced, significantly lowered sensitivity to the inhibitors malate and aspartate. K(0.5) for phosphoenolpyruvate is lower than wild-type value
R183Q
-
mutation results in complete desensitization to glucose 6-phosphate, heterotrophic effect of glucose 6-phosphate on the allosteric inhibitor L-malate is abolished. Sensitivity to the allosteric activator Gly is not affected
R183Q/R184Q
-
mutation results in complete desensitization to glucose 6-phosphate
R184Q
-
mutation results in complete desensitization to glucose 6-phosphate
R226Q
-
maximal activation caused by glycine is greatly reduced, significantly lowered sensitivity to the inhibitors malate and aspartate. K(0.5) for phosphoenolpyruvate is significantly higher than that of wild-type enzyme
R231A
-
decreased apparent affinity for the activator glucose 6-phosphate
R232Q
-
decreased apparent affinity for the activator glucose 6-phosphate, reduced apparent affinity for the activator glycine
R372Q
-
mutation results in a marked decrease in sensitivity to glucose 6-phosphate
additional information
Amaranthus edulis
-
heterozygous (Pp) and homozygous (pp) forms of a PEPC-deficient mutant of the C4 dicot Amaranthus edulis are analysed; rates of CO2 assimilation in air drop to 78% and 10% of the wild-type values in heterozygous and homozygous mutants, respectively. Stomatal conductance in air (531 microbar CO2) is similar in the wild-type and heterozygous mutant but the homozygous mutant has only 41% of the wild-type steady-state conductance under white light and the stomata opens more slowly in response to increased light or reduced CO2 partial pressure, suggesting that the C4 PEPC isoform plays an essential role in stomatal opening. Little difference in delta13C between the heterozygous mutant and wild type, indicating that leakiness, the ratio of CO2 leak rate out of the bundle sheath to the rate of CO2 supply by the C4 cycle, a measure of the coordination of C4 photosynthesis, is not affected by a 60% reduction in PEPC activity
R703G/R703G
P00864
mutant enzyme Arg703Gly/Arg704Gly shows a 20fold decreased turnover number compared to the wild type enzyme
additional information
-, O23946
at the rapid elongation phase of 10 days after anthesis, the PEPC activity in the monogenic, dominant cotton mutant Ligon lintless is only 25% of the wild type, which corresponded to about 55% reduction of fibre length
G961V
P15804
kcat: 7.2/sec (phosphoenolpyruvate), 8.5% of wild type catalytic activity
additional information
P15804
it is shown that even a modest, neutral alteration of the PEPC C-terminal hydrogen atom side chain is detrimental to enzyme function
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
agriculture
-
PEPC activated in the Brachiaria hybrid under low-P and low-pH conditions may contribute to the plants greater adaptation to tropical acid soils with P-low availability
biotechnology
-
elevated acetate concentrations have an inhibitory effect on growth rate and recombinant protein yield, and thus elimination of acetate formation is an important aim towards industrial production of recombinant proteins
agriculture
-
the PEPC gene and photosynthetic characteristics of PEPC transgenic rice can be stably transferred to the hybrid progenies, which might open a new breeding approach to the integration of conventional hybridization and biological technology
biotechnology
-
phosphoenolpyruvate carboxylase and Lactococcus lactis pyruvate carboxylase are overexpressed in Escherichia coli concurrently to improve the production of succinate. This coexpression system is also applied to mutant strains of Escherichia coli strategically designed by inactivating the competing pathways of succinate formation