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Information on EC 5.4.99.18 - 5-(carboxyamino)imidazole ribonucleotide mutase and Organism(s) Acetobacter aceti and UniProt Accession Q2QJL3

for references in articles please use BRENDA:EC5.4.99.18
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EC Tree
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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Acetobacter aceti
UNIPROT: Q2QJL3
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Word Map
The taxonomic range for the selected organisms is: Acetobacter aceti
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
H89 is not essential and does not function as part of a proton relay system. For synthesis of 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate, the carboxylate moiety is positioned in a small pocket proposed to facilitate nucleotide decarboxylation. In the reverse direction, enzyme favors protonation of 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate C4
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0007 - 0.2
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0006 - 12.2
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36
pH 8.0, 37°C, direction of decarboxylation of 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q2QJL3_ACEAC
182
0
18735
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18864
8 * 18900, calculated, 8 * 21000, SDS-PAGE, 8 * 18864, ESI-MS
18900
8 * 18900, calculated, 8 * 21000, SDS-PAGE, 8 * 18864, ESI-MS
197000
gel filtration
21000
8 * 18900, calculated, 8 * 21000, SDS-PAGE, 8 * 18864, ESI-MS
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
8 * 18900, calculated, 8 * 21000, SDS-PAGE, 8 * 18864, ESI-MS
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
multiple REDOR NMR studies of a 151000 Da complex of uniformly 15N-labeled enzyme and the active site ligand [6-13C]-citrate show a single ionization equilibrium associated with the key histidine H59. H59 exists in approximately equimolar amounts of an Ndelta-unprotonated pyridine-like form and an Ndelta-protonated pyrrole-like form. Proton transfer mechanism involves H59 Ndelta
hanging-drop method, crystals grow best at 295 K with the optimized mother-liquor conditions of 21-23% PEG 4K, 0.19 M ammonium acetate and 90 mM citrate, pH 5.25-5.5. Crystals belong to space group I422, with unit-cell parameters a = 99.25, c = 164.81 A
-
mutant H59N soaked in 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate, protonation of 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate C4 may occur in absence of H59
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H59D
0.16% of wild-type activity
H59N
inactive, crystallization data
H59Q
almost inactive
H89D
4.4% of wild-type activity
H89F
14% of wild-type activity
H89G
91% of wild-type activity
H89N
2.9% of wild-type activity
H89V
17% of wild-type activity
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
maximum of enzyme stability near pH 7.0
678203
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85
melting temperature
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme is active in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Settembre, E.C.; Chittuluru, J.R.; Mill, C.P.; Kappock, T.J.; Ealick, S.E.
Acidophilic adaptations in the structure of Acetobacter aceti N5-carboxyaminoimidazole ribonucleotide mutase (PurE)
Acta Crystallogr. Sect. D
60
1753-1760
2004
Acetobacter aceti
Manually annotated by BRENDA team
Constantine, C.Z.; Starks, C.M.; Mill, C.P.; Ransome, A.E.; Karpowicz, S.J.; Francois, J.A.; Goodman, R.A.; Kappock, T.J.
Biochemical and structural studies of N5-carboxyaminoimidazole ribonucleotide mutase from the acidophilic bacterium Acetobacter aceti
Biochemistry
45
8193-8208
2006
Acetobacter aceti (Q2QJL2), Acetobacter aceti
Manually annotated by BRENDA team
Schaefer, J.; Jiang, H.; Ransome, A.E.; Kappock, T.J.
Multiple active site histidine protonation states in Acetobacter aceti N5-carboxyaminoimidazole ribonucleotide mutase detected by REDOR NMR
Biochemistry
46
9507-9512
2007
Acetobacter aceti (Q2QJL3), Acetobacter aceti
Manually annotated by BRENDA team