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Information on EC 2.7.8.23 - carboxyvinyl-carboxyphosphonate phosphorylmutase
for references in articles please use BRENDA:EC2.7.8.23
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.8 Transferases for other substituted phosphate groups
2.7.8.23 carboxyvinyl-carboxyphosphonate phosphorylmutase
IUBMB Comments
Catalyses the transfer and decarboxylation of the carboxy(hydroxy)phosphoryl group, HOOC-P(O)(OH)- (phosphoryl being a 3-valent group), in the formation of an unusual C-P bond that is involved in the biosynthesis of the antibiotic bialaphos.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
showSynonyms
cpep phosphonomutase, carboxyphosphoenolpyruvate mutase, carboxyphosphonoenolpyruvate phosphonomutase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
carboxyphosphonoenolpyruvate phosphonomutase
-
-
-
-
CPEP mutase
CPEP phosphonomutase
-
-
-
-
CPEP mutase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1-carboxyvinyl carboxyphosphonate = 3-(hydroxyphosphinoyl)pyruvate + CO2
catalyses the transfer and decarboxylation of the carboxy(hydroxy)phosphoryl group, HOOC-P(O)(OH)-(phosphoryl being a 3-valent group), in the formation of an unusual C-P bond that is involved in the biosynthesis of the antibiotic bialaphos
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
substituted phospho group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
phosalacine biosynthesis, phosphinothricin tripeptide biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
1-carboxyvinyl carboxyphosphonate phosphorylmutase (decarboxylating)
Catalyses the transfer and decarboxylation of the carboxy(hydroxy)phosphoryl group, HOOC-P(O)(OH)- (phosphoryl being a 3-valent group), in the formation of an unusual C-P bond that is involved in the biosynthesis of the antibiotic bialaphos.
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CAS REGISTRY NUMBER
COMMENTARY
122799-57-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-carboxyvinyl carboxyphosphonate
3-(hydrohydroxyphosphoryl)pyruvate + CO2
Substrates: -
Products: -
Products: -
?
carboxyphosphinopyruvate
(hydroxyphosphinyl)pyruvate + CO2
-
Substrates: -
Products: -
Products: -
?
carboxyphosphoenolpyruvate
?
-
Substrates: -
Products: -
Products: -
?
carboxyphosphonoenolpyruvate
(hydroxyphosphinyl)pyruvate + CO2
-
Substrates: -
Products: -
Products: -
?
carboxyphosphonoenolpyruvate
(hydroxyphosphinyl)pyruvate + CO2
-
Substrates: catalyzes the rearrangement of the carboxyphosphonogroup to form the C-P bond of phosphinopyruvate
Products: -
Products: -
?
carboxyphosphonoenolpyruvate
(hydroxyphosphinyl)pyruvate + CO2
-
Substrates: first natural phosphinate
Products: -
Products: -
?
carboxyphosphonoenolpyruvate
(hydroxyphosphinyl)pyruvate + CO2
-
Substrates: biosynthetic pathway that leads to the tripeptide antibiotic bialaphos, formation of one of the two C-P bonds in bialaphos
Products: -
Products: -
?
carboxyphosphonoenolpyruvate
(hydroxyphosphinyl)pyruvate + CO2
-
Substrates: -
Products: -
Products: -
?
carboxyphosphonoenolpyruvate
(hydroxyphosphinyl)pyruvate + CO2
-
Substrates: first natural phosphinate
Products: -
Products: -
?
carboxyphosphonoenolpyruvate
(hydroxyphosphinyl)pyruvate + CO2
-
Substrates: biosynthetic pathway that leads to the tripeptide antibiotic bialaphos, formation of one of the two C-P bonds in bialaphos
Products: -
Products: -
?
carboxyphosphonoenolpyruvate
(hydroxyphosphinyl)pyruvate + CO2
-
Substrates: catalyzes the rearrangement of the carboxyphosphonogroup to form the C-P bond of phosphinopyruvate
Products: -
Products: -
?
carboxyphosphonoenolpyruvate
(hydroxyphosphinyl)pyruvate + CO2
-
Substrates: biosynthetic pathway that leads to the tripeptide antibiotic bialaphos, formation of one of the two C-P bonds in bialaphos
Products: -
Products: -
?
carboxyphosphonoenolpyruvate
(hydroxyphosphinyl)pyruvate + CO2
-
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-carboxyvinyl carboxyphosphonate
3-(hydrohydroxyphosphoryl)pyruvate + CO2
Substrates: -
Products: -
Products: -
?
carboxyphosphonoenolpyruvate
(hydroxyphosphinyl)pyruvate + CO2
-
Substrates: -
Products: -
Products: -
?
carboxyphosphonoenolpyruvate
(hydroxyphosphinyl)pyruvate + CO2
-
Substrates: first natural phosphinate
Products: -
Products: -
?
carboxyphosphonoenolpyruvate
(hydroxyphosphinyl)pyruvate + CO2
-
Substrates: biosynthetic pathway that leads to the tripeptide antibiotic bialaphos, formation of one of the two C-P bonds in bialaphos
Products: -
Products: -
?
carboxyphosphonoenolpyruvate
(hydroxyphosphinyl)pyruvate + CO2
-
Substrates: first natural phosphinate
Products: -
Products: -
?
carboxyphosphonoenolpyruvate
(hydroxyphosphinyl)pyruvate + CO2
-
Substrates: biosynthetic pathway that leads to the tripeptide antibiotic bialaphos, formation of one of the two C-P bonds in bialaphos
Products: -
Products: -
?
carboxyphosphonoenolpyruvate
(hydroxyphosphinyl)pyruvate + CO2
-
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
additional information
-
NaCl, KCl and NH4(SO4)2 up to 100 mM have no effect
Mn2+
-
increases activity, about 10times more active compared with the activity in presence of Mg2+
Mn2+
-
1 mM MnSO4, relative activity 680%, 10 mM MnSO4, relative activity 600%
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
-
enzyme is inactive in presence of EDTA, but inhibition is completely relieved by addition of 1 mM MnSO4 or MgSO4
additional information
-
phosphoenolpyruvate shows almost no effect
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
specific activity 217.0 U/mg of protein, one unit is the amount of enzyme required to produce 1micromol of bialaphos
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
the enzyme plays a role that is related to the tillering regulation in rice
physiological function
between a heat-tolerant strain (HTS) and heat-sensitive coisogenic rice strain (HSS), following short-term extreme high nighttime temperature stress at the first stage of seed ripening, 56 genes are differentially expressed. Unique SNPs located on the genes peroxidase precursor, glutathione S-transferase GSTU6, glycosyl hydrolases, carboxyvinylcarboxyphosphonate phosphorylmutase, and prolamin precursor PROLM3 are present in HTS but absent from HSS and show slight alterations in gene expression between HTS and HSS. Carboxyvinyl-carboxyphosphonate phosphorylmutase is downregulated 1.37fold in HTS but upregulated 7.50fold in HSS
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CPPM_ARATH
339
0
36566
Swiss-Prot
other Location (Reliability: 2)
CPPM_STRHY
295
0
32781
Swiss-Prot
other Location (Reliability: 3)
D6XBS8_STRX2
Streptomyces sviceus (strain ATCC 29083 / DSM 924 / JCM 4929 / NBRC 13980 / NCIMB 11184 / NRRL 5439 / UC 5370)
296
0
32796
TrEMBL
-
D9XF37_STRVT
Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494)
296
0
32774
TrEMBL
-
Q5IW33_STRVR
296
0
32774
TrEMBL
other Location (Reliability: 4)
Q8NRI8_CORGL
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
254
0
26586
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 80% ammonium sulfate suspension, no loss of activity observed for 1 month
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene cloned from a subgenomic library cloned by colony hybridisation in Escherichia coli AG1, subcloned into vector pET11a and overexpressed in Escherichia coli BL21(DE3)
-
nucleotide sequence of gene isolated and cloned and expressed in Streptomyces lividans 66 using expression vector pIJ680
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
agriculture
-
formation of one of the two C-P bonds in the tripeptide antibiotic bialaphos, a potent herbicide isolated from Streptomyces hygroscopicus SF1293, enzyme is produced in large amounts by high producer strain HP5-29, enzyme may contribute to improvement of bialphos production
agriculture
-
formation of one of the two C-P bonds in the tripeptide antibiotic bialaphos, a potent herbicide isolated from Streptomyces hygroscopicus SF1293, enzyme is produced in large amounts by high producer strain HP5-29, enzyme may contribute to improvement of bialphos production
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hidaka, T.; Hara, O.; Imai, S.; Anzai, H.; Murakami, T.; Nakaoka, K.; Seto, H.
Biochemical mechanism of C-P bond formation of bialaphos: use of gene manipulation for the analysis of the C-P bond formation step
Agric. Biol. Chem.
54
2121-2125
1990
no activity in Streptomyces hygroscopicus, Streptomyces hygroscopicus, Streptomyces hygroscopicus SF1293
brenda
Hidaka, T.; Imai, S.; Hara, O.; Anzai, H.; Murakami, T.; Nagaoka, K.; Seto, H.
Carboxyphosphoenolpyruvate phosphonomutase, a novel enzyme catalyzing C-P bond formation
J. Bacteriol.
172
3066-3072
1990
Streptomyces hygroscopicus, Streptomyces hygroscopicus SF1293
brenda
Hidaka, T.; Seto, H.
Comparison of two C-P bond-forming enzymes involved in the biosynthesis of bialaphos
Agric. Biol. Chem.
54
2467-2468
1990
Streptomyces hygroscopicus, Streptomyces hygroscopicus SF1293
-
brenda
Freeman, S.; Pollack, S.J.; Knowles, J.R.
Synthesis of the unusual metabolite carboxyphosphoenolpyruvate. Cloning and expression of carboxyphosphonoenolpyruvate mutase
J. Am. Chem. Soc.
114
377-378
1992
Streptomyces hygroscopicus
-
brenda
Hidaka, T.; Hidaka, M.; Uozumi, T.; Seto, H.
Nucleotide sequence of a carboxyphosphoenolpyruvate phosphonomutase gene isolated from a bialaphos-producing organism, Streptomyces hygroscopicus, and its expression in Streptomyces lividans
Mol. Gen. Genet.
233
476-478
1992
Streptomyces hygroscopicus
brenda
Pollack, S.J.; Freeman, S.; Pompliano, D.L.; Knowles, F.R.
Cloning, overexpression and mechanistic studies of carboxyphosphoenolpyruvate mutase from Streptomyces hygroscopicus
Eur. J. Biochem.
209
735-743
1992
no activity in Streptomyces hygroscopicus, Streptomyces hygroscopicus
brenda
Chen, F.; Jiang, L.; Zheng, J.; Huang, R.; Wang, H.; Hong, Z.; Huang, Y.
Identification of a co-segregative protein associated with the tillering trait in rice (Oryza sativa L.)
Plant OMICS
6
36-45
2013
Oryza sativa (Q2QWN6)
-
brenda
Zhou, H.; Zhang, H.; Wang, Z.; He, C.; You, L.; Fu, D.; Song, J.; Huang, Y.; Liao, J.
Discovery of unique single nucleotide polymorphisms in rice in response to high nighttime temperature stress using a hybrid sequencing strategy
Environ. Exp. Bot.
162
48-57
2019
Oryza sativa Japonica Group (Q2QWN6)
-
brenda
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