Information on EC 4.1.1.82 - phosphonopyruvate decarboxylase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.1.1.82
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RECOMMENDED NAME
GeneOntology No.
phosphonopyruvate decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-phosphonopyruvate = 2-phosphonoacetaldehyde + CO2
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2-aminoethylphosphonate biosynthesis
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Biosynthesis of antibiotics
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dehydrophos biosynthesis
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fosfomycin biosynthesis
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Metabolic pathways
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Microbial metabolism in diverse environments
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phosalacine biosynthesis
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phosphinothricin tripeptide biosynthesis
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Phosphonate and phosphinate metabolism
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rhizocticin A and B biosynthesis
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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].
CAS REGISTRY NUMBER
COMMENTARY hide
151662-34-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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swissprot
Manually annotated by BRENDA team
strain Tü494
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
2-phosphonoacetaldehyde + CO2
show the reaction diagram
pyruvate
acetaldehyde + CO2
show the reaction diagram
0.5% of 3-phosphonopyruvate kcat
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?
sulfopyruvate
sulfoacetaldehyde + CO2
show the reaction diagram
0.5% of 3-phosphonopyruvate kcat
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?
additional information
?
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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
3-phosphonopyruvate
2-phosphonoacetaldehyde + CO2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
sulfopyruvate
competitive inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0032 - 3.02
3-phosphonopyruvate
0.078
Ca2+
25°C, pH 7.3
0.082
Mg2+
25°C, pH 7.3
0.013
Mn2+
25°C, pH 7.3
0.013
thiamine diphosphate
25°C, pH 7.3
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.31 - 10.2
3-phosphonopyruvate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
sulfopyruvate
25°C, pH 7.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36000
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4 * 36000, SDS-PAGE
40000
3 * 40000, SDS-PAGE
41000
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x * 41000, deduced from nucleotide sequence
41199
3 * 41199, MALDI-TOF mass spectroscopy
43600
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2 * 43600, gel filtration
46000
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2 * 46000, gel filtration
72100
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gel filtration
120000
gel filtration
135000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
tetramer
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4 * 36000, SDS-PAGE
trimer
3 * 40000, SDS-PAGE; 3 * 41199, MALDI-TOF mass spectroscopy
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C and 4°C, half-life of 50 days
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4°C, 50 mM Tris-HCl, pH 7.5, 3 weeks, no loss of activity
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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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Ni-NTA column chromatography
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recombinant Ppyr decarboxylase, ammonium sulfate, DEAE-Sepahrose, hydroxylapatite
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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expression in Escherichia coli
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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D258A
9% of wild-type kcat for 3-phosphonopyruvate
D260A
0.1% of wild-type kcat for 3-phosphonopyruvate
E213A
5% of wild-type kcat for 3-phosphonopyruvate
D297E
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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
H110A
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no detectable activity
H111A
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the mutation has no significant influence on the steady state kinetic constants compared to the wild type enzyme
S25D
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catalytic turnover rate is 4fold less and Km is increased 460fold compared to the wild type enzyme
S25N
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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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H110A
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no detectable activity
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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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Show AA Sequence (166 entries)
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