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Information on EC 4.1.1.21 - phosphoribosylaminoimidazole carboxylase and Organism(s) Treponema denticola and UniProt Accession Q73PV9

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.21 phosphoribosylaminoimidazole carboxylase
IUBMB Comments
While this is the reaction that occurs in vertebrates during purine biosynthesis, two enzymes are required to carry out the same reaction in Escherichia coli, namely EC 6.3.4.18, 5-(carboxyamino)imidazole ribonucleotide synthase and EC 5.4.99.18, 5-(carboxyamino)imidazole ribonucleotide mutase . 5-Carboxyamino-1-(5-phospho-D-ribosyl)imidazole is not a substrate.
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This record set is specific for:
Treponema denticola
UNIPROT: Q73PV9
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Word Map
  • 4.1.1.21
  • saicars
  • n5-cair
  • phosphoribosylaminoimidazolesuccinocarboxamide
  • 4-carboxy-5-aminoimidazole
  • 6.3.2.6
  • aircs
  • n5-carboxyaminoimidazole
  • samdc
  • analysis
The taxonomic range for the selected organisms is: Treponema denticola
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
paics, phosphoribosylaminoimidazole carboxylase, air carboxylase, class ii pure, phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase, aminoimidazole ribonucleotide carboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AIR carboxylase
-
5-Amino-1-ribosylimidazole 5-phosphate carboxylase
-
-
-
-
5-Phosphoribosyl-5-aminoimidazole carboxylase
-
-
-
-
AIR carboxylase
-
-
-
-
AIRC
-
-
-
-
Carboxylyase, phosphoribosylaminoimidazole
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylation
-
-
-
-
decarboxylation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate carboxy-lyase [5-amino-1-(5-phospho-D-ribosyl)imidazole-forming]
While this is the reaction that occurs in vertebrates during purine biosynthesis, two enzymes are required to carry out the same reaction in Escherichia coli, namely EC 6.3.4.18, 5-(carboxyamino)imidazole ribonucleotide synthase and EC 5.4.99.18, 5-(carboxyamino)imidazole ribonucleotide mutase [3]. 5-Carboxyamino-1-(5-phospho-D-ribosyl)imidazole is not a substrate.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-04-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-carboxy-5-aminoimidazole ribonucleotide + H+
5-aminoimidazole ribonucleotide + CO2
show the reaction diagram
-
-
-
r
5-aminoimidazole ribonucleotide + CO2
4-carboxy-5-aminoimidazole ribonucleotide + H+
show the reaction diagram
-
-
-
r
additional information
?
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0038 - 0.009
4-carboxy-5-aminoimidazole ribonucleotide
0.06
5-aminoimidazole ribonucleotide
50 mM Tris-HCl (pH 8.0), at 10°C
13
CO2
50 mM Tris-HCl (pH 8.0), at 10°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16 - 65
4-carboxy-5-aminoimidazole ribonucleotide
77
CO2
50 mM Tris-HCl (pH 8.0), at 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
33
4-carboxy-5-aminoimidazole ribonucleotide
50 mM Tris-HCl (pH 8.0), at 30°C
6.4
5-aminoimidazole ribonucleotide
50 mM Tris-HCl (pH 8.0), at 10°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.7
calculated from amino acid sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17189
8 * 17189, calculated from amino acid sequence
17195
8 * 17195, ESI-MS
184000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homooctamer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 14-16% (w/v) PEG 1000, 100 mM MgCl2, and 100 mM imidazole (pH 8.0)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
T40N
the specific actzivity of the mutant is 20000fold lower than that of wild type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
streptomycin precipitation, ammonium sulfate precipitation, phenyl Sepharose 6 column chromatography, hydroxyapatite column chromatography, and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tranchimand, S.; Starks, C.M.; Mathews, I.I.; Hockings, S.C.; Kappock, T.J.
Treponema denticola PurE is a bacterial AIR carboxylase
Biochemistry
50
4623-4637
2011
Treponema denticola (Q73PV9), Treponema denticola
Manually annotated by BRENDA team