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Information on EC 5.4.99.18 - 5-(carboxyamino)imidazole ribonucleotide mutase and Organism(s) Escherichia coli and UniProt Accession P0AG18

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IUBMB Comments
In eubacteria, fungi and plants, this enzyme, along with EC 6.3.4.18, 5-(carboxyamino)imidazole ribonucleotide synthase, is required to carry out the single reaction catalysed by EC 4.1.1.21, phosphoribosylaminoimidazole carboxylase, in vertebrates . In the absence of EC 6.3.2.6, phosphoribosylaminoimidazolesuccinocarboxamide synthase, the reaction is reversible . The substrate is readily converted into 5-amino-1-(5-phospho-D-ribosyl)imidazole by non-enzymic decarboxylation .
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Escherichia coli
UNIPROT: P0AG18
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
n5-cair mutase, bapure, n5-carboxyaminoimidazole ribonucleotide mutase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
show the reaction diagram
common, buried carboxylate or CO2 binding site for substrate and product in a hydrophobic pocket, in which the carboxylate or CO2 interacts with backbone amides. The carboxylate orients the substrate for proton transfer from His45 to 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole to form an enzyme-bound aminoimidazole ribonucleotide and CO2 intermediate. subsequent movement of the aminoimidazole moiety reorients it for addition of CO2 at C4 to generate iso-5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate. H5 is now in a position to remove a C4 proton to produce 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole carboxymutase
In eubacteria, fungi and plants, this enzyme, along with EC 6.3.4.18, 5-(carboxyamino)imidazole ribonucleotide synthase, is required to carry out the single reaction catalysed by EC 4.1.1.21, phosphoribosylaminoimidazole carboxylase, in vertebrates [6]. In the absence of EC 6.3.2.6, phosphoribosylaminoimidazolesuccinocarboxamide synthase, the reaction is reversible [3]. The substrate is readily converted into 5-amino-1-(5-phospho-D-ribosyl)imidazole by non-enzymic decarboxylation [3].
CAS REGISTRY NUMBER
COMMENTARY hide
255379-40-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
show the reaction diagram
-
-
-
r
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
show the reaction diagram
-
-
-
r
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0226
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
wild-type, pH 7.5, 23°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0004 - 15.6
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
0.0021 - 15.5
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
126000
-
gel filtration
136000
-
sucrose density gradient ultracentrifugation
17000
-
8 * 17000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
-
8 * 17000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type cocrystallized with 4-nitroaminoimidazole ribonucleotide and mutants H45N and H45Q soaked with 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
hanging-drop vapor-diffusion method, crystals grown in the presence of 4-carboxaminoimidazole ribonucleotide belong to space group P2(1)2(1)2(1), with unit cell parameters a = 86.92, b = 94.55 and c = 149.96 A. The 1.5 A crystal structure reveals an octameric structure with 422 symmetry
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H45N
very low catalytic activity
H45Q
very low catalytic activity
H45W
very low catalytic activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Meyer, E.; Leonard, N.J.; Bhat, B.; Stubbe, J.; Smith, J.M.
Purification and characterization of the purE, purK, and purC gene products: identification of a previously unrecognized energy requirement in the purine biosynthetic pathway
Biochemistry
31
5022-5032
1992
Escherichia coli
Manually annotated by BRENDA team
Meyer, E.; Kappock, T.J.; Osuji, C.; Stubbe, J.
Evidence for the Direct Transfer of the carboxylate of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to generate 4-carboxy-5-aminoimidazole ribonucleotide catalyzed by Escherichia coli PurE, an N5-CAIR mutase
Biochemistry
38
3012-3018
1999
Escherichia coli
Manually annotated by BRENDA team
Mueller, E.J.; Meyer, E.; Rudolph, J.; Davisson, V.J.; Stubbe, J.
N5-carboxyaminoimidazole ribonucleotide: evidence for a new intermediate and two new enzymatic activities in the de novo purine biosynthetic pathway of Escherichia coli
Biochemistry
33
2269-2278
1994
Escherichia coli
Manually annotated by BRENDA team
Watanabe, W.; Sampei, G.; Aiba, A.; Mizobuchi, K.
Identification and sequence analysis of Escherichia coli purE and purK genes encoding 5'-phosphoribosyl-5-amino-4-imidazole carboxylase for de novo purine biosynthesis
J. Bacteriol.
171
198-204
1989
Escherichia coli, Escherichia coli NK6051
Manually annotated by BRENDA team
Mathews, I.I.; Kappock, T.J.; Stubbe, J.; Ealick, S.E.
Crystal structure of Escherichia coli PurE, an unusual mutase in the purine biosynthetic pathway
Structure
7
1395-1406
1999
Escherichia coli
Manually annotated by BRENDA team
Hoskins, A.A.; Morar, M.; Kappock, T.J.; Mathews, I.I.; Zaugg, J.B.; Barder, T.E.; Peng, P.; Okamoto, A.; Ealick, S.E.; Stubbe, J.
N5-CAIR mutase: role of a CO2 binding site and substrate movement in catalysis
Biochemistry
46
2842-2855
2007
Escherichia coli (P0AG18), Escherichia coli
Manually annotated by BRENDA team