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Information on EC 4.1.1.82 - phosphonopyruvate decarboxylase and Organism(s) Streptomyces hygroscopicus and UniProt Accession Q54271

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.82 phosphonopyruvate decarboxylase
IUBMB Comments
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 . It is the initial step in all of the major biosynthetic pathways of phosphonate natural products .
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Streptomyces hygroscopicus
UNIPROT: Q54271
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Word Map
The taxonomic range for the selected organisms is: Streptomyces hygroscopicus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
phosphonopyruvate decarboxylase, pnpy decarboxylase, ppyr decarboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PnPy decarboxylase
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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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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
3-phosphonopyruvate
2-phosphonoacetaldehyde + CO2
show the reaction diagram
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-
-
-
?
NATURAL SUBSTRATE
NATURAL 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
key enzyme in the biosynthesis of C-P bond compounds, overview
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-
ir
3-phosphonopyruvate
2-phosphonoacetaldehyde + CO2
show the reaction diagram
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-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
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-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required for activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene bcpC
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PPD_STRHY
401
0
41629
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
135000
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gel filtration
36000
-
4 * 36000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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4 * 36000, SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nakashita, H.; Kozuka, K.; Hidaka, T.; Hara, O.; Seto, H.
Identification and expression of the gene encoding phosphonopyruvate decarboxylase of Streptomyces hygroscopicus
Biochim. Biophys. Acta
1490
159-162
2000
Streptomyces hygroscopicus (Q54271), Streptomyces hygroscopicus
Manually annotated by BRENDA team
Nakashita, H.; Watanabe, K.; Hara, O.; Hidaka, T.; Seto, H.
Studies on the biosynthesis of bialaphos. Biochemical mechanism of C-P bond formation: discovery of phosphonopyruvate decarboxylase which catalyzes the formation of phosphonoacetaldehyde from phosphonopyruvate
J. Antibiot.
50
212-219
1997
Streptomyces hygroscopicus
Manually annotated by BRENDA team