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Enzyme Nomenclature
Information on EC 4.1.1.82 - phosphonopyruvate decarboxylase
for references in articles please use BRENDA:EC4.1.1.82
Word Map on EC 4.1.1.82
- 4.1.1.82
- streptomyces
- phosphoenolpyruvate
- wedmorensis
-
decarboxylation
- thiamin
- 2-aminoethylphosphonate
-
phosphomutase
- hygroscopicus
- bialaphos
- fosfomycin
- pep
- diphosphate
- sulfopyruvate
-
unfavorable
-
bacteroides
- phosphonate
- fragilis
-
abscess
- phosphinothricin
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
4.1.1.82
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RECOMMENDED NAME
GeneOntology No.
phosphonopyruvate decarboxylase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-phosphonopyruvate = 2-phosphonoacetaldehyde + CO2
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
3-phosphonopyruvate carboxy-lyase (2-phosphonoacetaldehyde-forming)
The enzyme catalyses a step in the biosynthetic pathway of 2-aminoethylphosphonate, a component of the capsular polysaccharide complex of Bacteroides fragilis. Requires thiamine diphosphate and Mg2+ as cofactors. The enzyme is activated by the divalent cations Mg2+, Ca2+ and Mn2+. Pyruvate and sulfopyruvate can also act as substrates, but more slowly. This enzyme drives the reaction catalysed by EC 5.4.2.9, phosphoenolpyruvate mutase, in the thermodynamically unfavourable direction of 3-phosphonopyruvate formation [2]. It is the initial step in all of the major biosynthetic pathways of phosphonate natural products [3].
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CAS REGISTRY NUMBER
COMMENTARY
151662-34-9
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pyruvate
acetaldehyde + CO2
0.5% of 3-phosphonopyruvate kcat
-
-
?
sulfopyruvate
sulfoacetaldehyde + CO2
0.5% of 3-phosphonopyruvate kcat
-
-
?
3-phosphonopyruvate
2-phosphonoacetaldehyde + CO2
key enzyme in the biosynthesis of C-P bond compounds, overview
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-
ir
3-phosphonopyruvate
2-phosphonoacetaldehyde + CO2
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-
-
?
3-phosphonopyruvate
2-phosphonoacetaldehyde + CO2
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-
-
?
3-phosphonopyruvate
2-phosphonoacetaldehyde + CO2
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-
-
-
?
additional information
?
-
-
neither pyruvate, beta-hydroxypyruvate, nor fluoropyruvate serve as alternative substrates
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-
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additional information
?
-
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neither pyruvate, beta-hydroxypyruvate, nor fluoropyruvate serve as alternative substrates
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-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-phosphonopyruvate
2-phosphonoacetaldehyde + CO2
Q54271
key enzyme in the biosynthesis of C-P bond compounds, overview
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-
ir
3-phosphonopyruvate
2-phosphonoacetaldehyde + CO2
O86938
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-
-
?
3-phosphonopyruvate
2-phosphonoacetaldehyde + CO2
O86938
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-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
thiamine diphosphate
-
primary sequence of Ppd contains signature typical for enzymes requiring thiamine diphosphate
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Mn2+
Mg2+
-
Mg2+ is required for activity, Ca2+ and Mn2+ can substitute for Mg2+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0032
3-phosphonopyruvate
25°C, pH 7.3, 5 mM MgCl2, 1 mM MnCl2, 0.2 mM thiamine pyrophosphate
0.0032
3-phosphonopyruvate
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wild type enzyme, at pH 8.0 (HEPES buffer) and at 30°C
0.013
3-phosphonopyruvate
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mutant enzyme H111A, at pH 8.0 (HEPES buffer) and at 30°C
0.04
3-phosphonopyruvate
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mutant enzyme D297E, at pH 8.0 (HEPES buffer) and at 30°C
0.25
3-phosphonopyruvate
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mutant enzyme S25N, at pH 8.0 (HEPES buffer) and at 30°C
1.47
3-phosphonopyruvate
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mutant enzyme S25D, at pH 8.0 (HEPES buffer) and at 30°C
3.02
3-phosphonopyruvate
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mutant enzyme D297N, at pH 8.0 (HEPES buffer) and at 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.31
3-phosphonopyruvate
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mutant enzyme S25D, at pH 8.0 (HEPES buffer) and at 30°C
0.55
3-phosphonopyruvate
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mutant enzyme D297N, at pH 8.0 (HEPES buffer) and at 30°C
0.76
3-phosphonopyruvate
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mutant enzyme D297E, at pH 8.0 (HEPES buffer) and at 30°C
0.78
3-phosphonopyruvate
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mutant enzyme S25N, at pH 8.0 (HEPES buffer) and at 30°C
1.18
3-phosphonopyruvate
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wild type enzyme, at pH 8.0 (HEPES buffer) and at 30°C
1.24
3-phosphonopyruvate
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mutant enzyme H111A, at pH 8.0 (HEPES buffer) and at 30°C
10.2
3-phosphonopyruvate
25°C, pH 7.3, 5 mM MgCl2, 1 mM MnCl2, 0.2 mM thiamine diphosphate
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
trimer
3 * 40000, SDS-PAGE; 3 * 41199, MALDI-TOF mass spectroscopy
homodimer
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2 * 43600, gel filtration; 2 * 46000, gel filtration
homodimer
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2 * 43600, gel filtration; 2 * 46000, gel filtration
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, DEAE-cellulose, TSK-gel Phenyl-5PW, gel filtration, Mono Q
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recombinant Ppyr decarboxylase, ammonium sulfate, DEAE-Sepahrose, hydroxylapatite
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as a recombinant fusion protein with an N-terminal 10x histidine-tag in Escherichia coli BL21(DE3) cells
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gene bcpC, located in the bialaphos biosynthetic gene cluster, DNA and amino acid sequence determination and analysis, complementation of an enzyme-deficient mutant strain of Streptomyces wedmorensis NP-7, enzyme expression in Streptomyces lividans
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D297E
-
catalytic turnover rate is 1.5fold less and Km is increased about 13fold compared to the wild type enzyme
D297N
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catalytic turnover rate of D297N is 2fold lower and Km is increased 940fold compared to the wild type enzyme
G94A
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compared to wild type PPDC, Km is increased only 2fold, while kcat is 4fold lower
H111A
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the mutation has no significant influence on the steady state kinetic constants compared to the wild type enzyme
S25D
-
catalytic turnover rate is 4fold less and Km is increased 460fold compared to the wild type enzyme
S25N
-
catalytic turnover rate is 1.5fold less and Km is increased 80fold compared to the wild type enzyme
D297N
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catalytic turnover rate of D297N is 2fold lower and Km is increased 940fold compared to the wild type enzyme
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G94A
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compared to wild type PPDC, Km is increased only 2fold, while kcat is 4fold lower
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H111A
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the mutation has no significant influence on the steady state kinetic constants compared to the wild type enzyme
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S25D
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catalytic turnover rate is 4fold less and Km is increased 460fold compared to the wild type enzyme
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LINKS TO OTHER DATABASES (specific for EC-Number 4.1.1.82)
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