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
5.4.2.9
-
RECOMMENDED NAME
GeneOntology No.
phosphoenolpyruvate mutase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
phosphoenolpyruvate = 3-phosphonopyruvate
show the reaction diagram
involved in the biosynthesis of the C-P bond, although the equilibrium greatly favours phosphoenolpyruvate
-
-
-
phosphoenolpyruvate = 3-phosphonopyruvate
show the reaction diagram
mechanism
-
phosphoenolpyruvate = 3-phosphonopyruvate
show the reaction diagram
mechanism
-
phosphoenolpyruvate = 3-phosphonopyruvate
show the reaction diagram
stereochemistry
-
phosphoenolpyruvate = 3-phosphonopyruvate
show the reaction diagram
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
group transfer
-
-
intramolecular, phosphate group
-
isomerization
-
-
-
-
isomerization
-
-
PATHWAY
KEGG Link
MetaCyc Link
2-aminoethylphosphonate biosynthesis
-
Biosynthesis of secondary metabolites
-
dehydrophos biosynthesis
-
fosfomycin biosynthesis
-
FR-900098 and FR-33289 antibiotics biosynthesis
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
phosphinothricin tripeptide biosynthesis
-
Phosphonate and phosphinate metabolism
-
SYSTEMATIC NAME
IUBMB Comments
phosphoenolpyruvate 2,3-phosphonomutase
Involved in the biosynthesis of the C-P bond, although the equilibrium greatly favours phosphoenolpyruvate.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
carboxyphosphoenolpyruvate phosphonomutase
-
-
-
-
PEP mutase
-
-
-
-
PEP mutase
-
-
PEP phosphomutase
-
-
-
-
PEPPM
-
-
-
-
phosphoenolpyruvate mutase
-
-
-
-
phosphoenolpyruvate mutase
-
-
phosphoenolpyruvate phosphomutase
-
-
-
-
phosphomutase, phosphoenolpyruvate-phosphonopyruvate
-
-
-
-
CPEP phosphonomutase
-
-
-
-
additional information
-
phosphoenolpyruvate phosphomutase and carboxyphosphoenolpyruvate phosphonomutase are distinct enzymes which are highly specific to their own substrates
additional information
Streptomyces hygroscopicus SF1293
-
phosphoenolpyruvate phosphomutase and carboxyphosphoenolpyruvate phosphonomutase are distinct enzymes which are highly specific to their own substrates
-
CAS REGISTRY NUMBER
COMMENTARY
115756-49-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
phosphonoalanine-induced
-
-
Manually annotated by BRENDA team
Burkholderia gladioli B-1
B-1
-
-
Manually annotated by BRENDA team
expression in Streptomyces lividans; SF1293
-
-
Manually annotated by BRENDA team
mutant NP71; SF1293; similar enzyme
-
-
Manually annotated by BRENDA team
phosphoenolpyruvate phosphomutase and carboxyphosphoenolpyruvate phosphonomutase are distinct enzymes which are highly specific to their own substrates; SF1293; similar enzyme
-
-
Manually annotated by BRENDA team
Streptomyces hygroscopicus SF1293
SF1293
-
-
Manually annotated by BRENDA team
ATCC 151905
-
-
Manually annotated by BRENDA team
overexpression in Escherichia coli
-
-
Manually annotated by BRENDA team
expressed during epimastygote, trypomastigote, mammalian amastigote stage
SwissProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-phosphonopyruvate
phosphoenolpyruvate
show the reaction diagram
-
-
-
-
r
carboxyphosphoenolpyruvate
phosphinopyruvate + CO2
show the reaction diagram
-
-
-
?
carboxyphosphoenolpyruvate
phosphinopyruvate + CO2
show the reaction diagram
-
similar enzyme, phosphoenolpyruvate phosphomutase and carboxyphosphoenolpyruvate phosphonomutase are distinct enzymes which are highly specific to their own substrates
-
?
carboxyphosphoenolpyruvate
phosphinopyruvate + CO2
show the reaction diagram
Streptomyces hygroscopicus SF1293
-
-
-
?
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
-
-
-
r
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
-
-
-
r
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
-
-
-
-
r
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
Q8T8D9, -
-
-
-
-
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
-
equilibrium greatly favours phosphoenolpyruvate
-
r
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
-
equilibrium greatly favours phosphoenolpyruvate
-
-
r
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
-
equilibrium greatly favours phosphoenolpyruvate
-
r
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
-
equilibrium greatly favours phosphoenolpyruvate
-
?
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
-
equilibrium greatly favours phosphoenolpyruvate
-
?
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
-
phosphoenolpyruvate phosphomutase and carboxyphosphoenolpyruvate phosphonomutase are distinct enzymes which are highly specific to their own substrates
-
?
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
-
involved in the biosynthesis of the C-P bond, although the equilibrium greatly favours phosphoenolpyruvate
-
-
r
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
-
enzyme catalyzes the formation of a C-P bond that is involved in the biosynthesis of the antibiotic bialaphos, i.e. SF-1293
-
-
?
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
Streptomyces hygroscopicus SF1293
-
enzyme catalyzes the formation of a C-P bond that is involved in the biosynthesis of the antibiotic bialaphos, i.e. SF-1293
-
-
?
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
Streptomyces hygroscopicus SF1293
-
equilibrium greatly favours phosphoenolpyruvate, phosphoenolpyruvate phosphomutase and carboxyphosphoenolpyruvate phosphonomutase are distinct enzymes which are highly specific to their own substrates
-
?
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
Streptomyces hygroscopicus SF1293
-
enzyme catalyzes the formation of a C-P bond that is involved in the biosynthesis of the antibiotic bialaphos, i.e. SF-1293
-
-
?
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
Streptomyces hygroscopicus SF1293
-
equilibrium greatly favours phosphoenolpyruvate
-
?
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
Streptomyces hygroscopicus SF1293
-
enzyme catalyzes the formation of a C-P bond that is involved in the biosynthesis of the antibiotic bialaphos, i.e. SF-1293
-
-
?
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
Streptomyces hygroscopicus SF1293
-
-
-
?
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
Burkholderia gladioli B-1
-
equilibrium greatly favours phosphoenolpyruvate
-
r
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
3-phosphonopyruvate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
-
involved in the biosynthesis of the C-P bond, although the equilibrium greatly favours phosphoenolpyruvate
-
-
r
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
-
enzyme catalyzes the formation of a C-P bond that is involved in the biosynthesis of the antibiotic bialaphos, i.e. SF-1293
-
-
?
phosphoenolpyruvate
3-phosphonopyruvate
show the reaction diagram
Streptomyces hygroscopicus SF1293
-
enzyme catalyzes the formation of a C-P bond that is involved in the biosynthesis of the antibiotic bialaphos, i.e. SF-1293
-
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
divalent metal ion required, 50% of the activation with Mg2+; Km: 0.002 mM
Co2+
-
Km: 0.0012 mM
Co2+
Q8T8D9, -
divalent cation required, in decreasing order of activitation: Mg2+, Co2+, Mn2+, Zn2+, Ni2+
Co2+
-
Km: 0.0003 mM
Mg2+
-
increases activity
Mg2+
-
absolutely required
Mg2+
-
divalent metal ion required: Mg2+, Co2+, Zn2+ or Mn2+, maximal activation with Mg2+; Km: 0.0058 mM
Mg2+
-
Km: 0.0035 mM
Mg2+
-
or Mn2+ required
Mg2+
Q8T8D9, -
absolutely required; divalent cation required, in decreasing order of activitation: Mg2+, Co2+, Mn2+, Zn2+, Ni2+; Km: 0.0084 mM
Mg2+
-
Km: 0.004 mM
Mn2+
-
activates
Mn2+
-
divalent metal ion required, 30% of the activation with Mg2+; Km: 0.007 mM
Mn2+
-
activates; Km: 0.000016 mM
Mn2+
-
or Mg2+ required
Mn2+
Q8T8D9, -
divalent cation required, in decreasing order of activitation: Mg2+, Co2+, Mn2+, Zn2+, Ni2+
Ni2+
Q8T8D9, -
divalent cation required, in decreasing order of activitation: Mg2+, Co2+, Mn2+, Zn2+, Ni2+
Ni2+
-
Km: 0.0022 mM
Zn2+
-
divalent metal ion required, 40% of the activation with Mg2+; Km: 0.007 mM
Zn2+
-
Km: 0.0015 mM
Zn2+
Q8T8D9, -
divalent cation required, in decreasing order of activitation: Mg2+, Co2+, Mn2+, Zn2+, Ni2+
Zn2+
-
Km: 0.00018
Mn2+
-
Km: 0.00011 mM
additional information
Q8T8D9, -
no activation by Ca2+
additional information
-
no activation by Ca2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
synergistic inhibition in combination with a small noncompetitive inhibitor
oxalate
-
competitive
oxalylphosphate
-
competitive
PO43-
-
competitive
SO32-
-
noncompetitive
SO42-
-
competitive
sulfopyruvate
-
-
VO43-
-
competitive
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0016
-
3-Phosphonopyruvate
-
wild-type, pH 7.5, 25C
0.0059
-
3-Phosphonopyruvate
-
mutant K120R, pH 7.5, 25C
0.038
-
3-Phosphonopyruvate
-
mutant N122A, pH 7.5, 25C
0.046
-
3-Phosphonopyruvate
-
mutant K120A, pH 7.5, 25C
0.06
-
3-Phosphonopyruvate
-
mutant L124A, pH 7.5, 25C
0.77
-
phosphoenolpyruvate
-
25C, pH 7.5
0.0016
-
Phosphonopyruvate
-
25C, pH 7.5
0.002
-
Phosphonopyruvate
-
pH 7.5
0.0032
-
Phosphonopyruvate
-
mutant N122D, 25C, pH 7.5
0.0035
-
Phosphonopyruvate
-
25C, pH 7.5
0.0065
-
Phosphonopyruvate
-
mutant H190A, 25C, pH 7.5
0.0078
-
Phosphonopyruvate
-
mutant D58N, 25C, pH 7.5
0.008
-
Phosphonopyruvate
Q8T8D9, -
25C, pH 8.0
0.01
-
Phosphonopyruvate
-
pH 7.5
0.019
-
Phosphonopyruvate
-
30C, pH 7.5
0.038
-
Phosphonopyruvate
-
mutant N122A, 25C, pH 7.5
0.054
-
Phosphonopyruvate
-
mutant R159A, 25C, pH 7.5
0.063
-
Phosphonopyruvate
-
truncated enzyme, pH 7.5
0.065
-
Phosphonopyruvate
-
pH 7.5
0.067
-
Phosphonopyruvate
-
30C, pH 7.7
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.006
-
3-Phosphonopyruvate
-
mutant N122A, pH 7.5, 25C
0.0098
-
3-Phosphonopyruvate
-
mutant L124A, pH 7.5, 25C
0.32
-
3-Phosphonopyruvate
-
mutant K120R, pH 7.5, 25C
0.34
-
3-Phosphonopyruvate
-
mutant K120A, pH 7.5, 25C
34
-
3-Phosphonopyruvate
-
wild-type, pH 7.5, 25C
38
-
Phosphonopyruvate
-
-
41
-
Phosphonopyruvate
-
30C, pH 7.7
60
-
Phosphonopyruvate
-
pH 7.5
71
-
Phosphonopyruvate
-
truncated enzyme
150
-
Phosphonopyruvate
-
pH 7.5
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.3
-
Mg2+
-
pH 7.5
0.025
-
oxalate
-
pH 7.5
0.032
-
oxalate
-
25C, pH 7.5
0.18
-
oxalylphosphate
-
25C, pH 7.5
0.022
-
sulfopyruvate
-
25C, pH 7.5
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
54
-
Q8T8D9, -
25C, pH 8.0
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-
similar enzyme
7.7
-
-
assay at
8
-
Q8T8D9, -
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
35
-
-
similar enzyme
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
27
-
-
27C: about 50% of maximum activity, 45C: about 70% of maximum activity
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Q8T8D9, -
large granule fraction
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
45000
67000
-
Streptomyces hygroscopicus SF1293, gel filtration, similar enzyme
69000
-
-
non-denaturing gel electrophoresis
81000
-
-
gel filtration
144000
-
-
gel filtration
220000
-
-
PAGE
263000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 32688, gene expressed in Escherichia coli, value deduced from DNA sequence
dimer
-
2 * 32000, SDS-PAGE, similar enzyme
dimer
-
2 * 33000, denaturing gel electrophoresis
dimer
-
2 * 38000, SDS-PAGE
dimer
Streptomyces hygroscopicus SF1293
-
2 * 32000, SDS-PAGE, similar enzyme
-
tetramer
-
4 * 61000, SDS-PAGE
tetramer
-
crystallization data
tetramer
-
4 * 34000, SDS-PAGE
tetramer
Burkholderia gladioli B-1
-
4 * 61000, SDS-PAGE
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
in complex with Mg2+-oxalate
-
of wild-type and mutant D58A, both in apo state and in complex with Mg2+
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
8
-
stable in this range, similar enzyme
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
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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 ACCESSION NO.
LITERATURE
extremely instable
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 50% glycerol, 25 mM potassium phosphate, pH 7
-
-80C, TEA buffer, pH 7.5, 10% glycerol, 4 weeks, minimal losses of activity
-
4C, TEA buffer, pH 7.5, 10% glycerol, 2 weeks, minimal losses of activity
-
-20C, 80% ammonium sulfate suspension, stable for 1 month, similar enzyme
-
4C, 50 mM MES buffer, pH 6.5, 1 mg protein/ml, stable for 1 week, 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
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
SF1293, mutant NP71; similar enzyme
-
overexpression in Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
a Streptomyces luridus library is constructed
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D58A
-
no enzymic activity
D58A
-
D58 functions in phosphoryl transfer
D58A
-
crystallization data
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
N122A
-
Km: 0.038 mM
N122A
-
25fold increase in Km-value
N122D
-
Km: 0.0032 mM
R159A
-
Km: 0.054 mM
R159A
-
R159 functions in phosphoenolpyruvate carboxylate binding