Information on EC 5.4.2.9 - phosphoenolpyruvate mutase

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

EC NUMBER
COMMENTARY hide
5.4.2.9
-
RECOMMENDED NAME
GeneOntology No.
phosphoenolpyruvate mutase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
phosphoenolpyruvate = 3-phosphonopyruvate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
group transfer
-
-
intramolecular, phosphate group
-
isomerization
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2-aminoethylphosphonate biosynthesis
-
-
Biosynthesis of antibiotics
-
-
dehydrophos biosynthesis
-
-
fosfomycin biosynthesis
-
-
FR-900098 and FR-33289 antibiotics biosynthesis
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
phosalacine biosynthesis
-
-
phosphinothricin tripeptide biosynthesis
-
-
Phosphonate and phosphinate metabolism
-
-
rhizocticin A and B biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
phosphoenolpyruvate 2,3-phosphonomutase
Involved in the biosynthesis of the C-P bond, although the equilibrium greatly favours phosphoenolpyruvate.
CAS REGISTRY NUMBER
COMMENTARY hide
115756-49-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
phosphonoalanine-induced
-
-
Manually annotated by BRENDA team
B-1
-
-
Manually annotated by BRENDA team
B-1
-
-
Manually annotated by BRENDA team
expressed during epimastygote, trypomastigote, mammalian amastigote stage
SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-phosphonopyruvate
phosphoenolpyruvate
show the reaction diagram
-
-
-
-
r
carboxyphosphoenolpyruvate
phosphinopyruvate + CO2
show the reaction diagram
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Br-
-
noncompetitive
Cl-
-
noncompetitive
H2PO2-
-
noncompetitive
HCO2-
-
noncompetitive
HCO3-
-
noncompetitive
HPO32-
-
competitive
I-
-
noncompetitive
isocitrate analogues
-
-
Mg2+-oxalate
-
-
NO2-
-
noncompetitive
NO3-
-
noncompetitive
oxalate
oxalylphosphate
-
competitive
PO43-
-
competitive
SO32-
-
noncompetitive
SO42-
-
competitive
sulfopyruvate
-
-
VO43-
-
competitive
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0016 - 0.06
3-phosphonopyruvate
0.77
phosphoenolpyruvate
-
25C, pH 7.5
0.0016 - 0.067
Phosphonopyruvate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006 - 34
3-phosphonopyruvate
38 - 150
Phosphonopyruvate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3
Mg2+
-
pH 7.5
0.025 - 0.032
oxalate
0.18
oxalylphosphate
-
25C, pH 7.5
0.022
sulfopyruvate
-
25C, pH 7.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
similar enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
similar enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27
-
27C: about 50% of maximum activity, 45C: about 70% of maximum activity
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
large granule fraction
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000 - 67000
-
Streptomyces hygroscopicus SF1293, gel filtration, similar enzyme
69000
-
non-denaturing gel electrophoresis
81000
-
gel filtration
144000
-
gel filtration
263000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 32688, gene expressed in Escherichia coli, value deduced from DNA sequence
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with Mg2+-oxalate
-
of wild-type and mutant D58A, both in apo state and in complex with Mg2+
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9
-
25C, 30 min, highest stability in this range, pH 9.1: 50% loss of activity, pH 5.2: complete loss of activity
648834
5.5 - 8
-
stable in this range, similar enzyme
643769
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
pH 7.5, 30 min, no loss of activity
30
-
pH 7.5, 30 min, 2% loss of activity
35
-
pH 7.5, 30 min, 51% loss of activity
40
-
pH 7.5, 30 min, 64% loss of activity
45
-
pH 7.5, 30 min, 71% loss of activity
50
-
pH 7.5, 30 min, 92% loss of activity
60
-
pH 7.5, 30 min, complete loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
extremely instable
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 50% glycerol, 25 mM potassium phosphate, pH 7
-
-20C, 80% ammonium sulfate suspension, stable for 1 month, similar enzyme
-
-20C, after quick freezing in a buffered solution, pH 7.5, 10% v/v glycerol, 50 mM triethanolamine, 0.5 mM DTT, 5 mM MgCl2, less than 20% loss of activity after 6 weeks
-
-80C, TEA buffer, pH 7.5, 10% glycerol, 4 weeks, minimal losses of activity
-
4C, 50 mM MES buffer, pH 6.5, 1 mg protein/ml, stable for 1 week, similar enzyme
-
4C, TEA buffer, pH 7.5, 10% glycerol, 2 weeks, minimal losses of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
-
SF1293, mutant NP71; similar enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a Streptomyces luridus library is constructed
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D58N
-
Km: 0.0078 mM
D58S
-
no enzymic activity
D85A
-
D85, D87, E114 function in Mg2+-binding
D87A
-
D85, D87, E114 function in Mg2+-binding
E114A
-
D85, D87, E114 function in Mg2+-binding
H190A
-
Km: 0.0065 mM
K120A
-
30fold increase in Km-value
K120R
-
3fold increase in Km-value
L124A
-
40fold increase in Km-value
N122D
-
Km: 0.0032 mM
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