Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.7.3.3 - factor-independent urate hydroxylase and Organism(s) Arthrobacter globiformis and UniProt Accession D0VWQ1

for references in articles please use BRENDA:EC1.7.3.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
This enzyme was previously thought to be a copper protein, but it is now known that the enzymes from soy bean (Glycine max), the mould Aspergillus flavus and Bacillus subtilis contains no copper nor any other transition-metal ion. The 5-hydroxyisourate formed decomposes spontaneously to form allantoin and CO2, although there is an enzyme-catalysed pathway in which EC 3.5.2.17, hydroxyisourate hydrolase, catalyses the first step. The enzyme is different from EC 1.14.13.113 (FAD-dependent urate hydroxylase).
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Arthrobacter globiformis
UNIPROT: D0VWQ1
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Arthrobacter globiformis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
uricase, rasburicase, urate oxidase, uricase ii, uric acid oxidase, uricozyme, aguox, nodulin 35, elitek, fasturtec, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N-35
-
-
-
-
Nodule specific uricase
-
-
-
-
Nodulin 35
-
-
-
-
Nodulin 35 homolog
-
-
-
-
Non-symbiotic uricase
-
-
-
-
oxidase, urate
-
-
-
-
Urate oxidase
uric acid oxidase
-
-
-
-
uricase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
urate:oxygen oxidoreductase
This enzyme was previously thought to be a copper protein, but it is now known that the enzymes from soy bean (Glycine max), the mould Aspergillus flavus and Bacillus subtilis contains no copper nor any other transition-metal ion. The 5-hydroxyisourate formed decomposes spontaneously to form allantoin and CO2, although there is an enzyme-catalysed pathway in which EC 3.5.2.17, hydroxyisourate hydrolase, catalyses the first step. The enzyme is different from EC 1.14.13.113 (FAD-dependent urate hydroxylase).
CAS REGISTRY NUMBER
COMMENTARY hide
9002-12-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
urate + O2 + H2O
5-hydroxyisourate + H2O2
show the reaction diagram
urate + O2 + H2O
5-hydroxyisourate + H2O2
show the reaction diagram
-
enzyme production is induced by addition of uric acid to the culture medium
-
-
?
urate + O2 + H2O
allantoin + H2O2
show the reaction diagram
-
-
-
-
?
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
urate + O2 + H2O
5-hydroxyisourate + H2O2
show the reaction diagram
urate + O2 + H2O
5-hydroxyisourate + H2O2
show the reaction diagram
-
enzyme production is induced by addition of uric acid to the culture medium
-
-
?
urate + O2 + H2O
allantoin + H2O2
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
enzyme contains copper, inhibited by excessive addition of Cu2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8-Azaxanthine
substrate analogue
Cu2+
-
enzyme contains copper, inhibited by excessive addition of Cu2+, 98% inhibition by 1 mM CuCl2, 97% inhibition by 1 mM CuSO4
ZnCl2
-
1 mM, 91% inhibition
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1045 - 0.1403
Urate
0.075
Urate
-
pH 7.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.8 - 6.64
Urate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
46.4 - 55.5
Urate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.96
-
isoelectric focusing, pH gradient 3.5-9.5
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
URIC_ARTGO
302
0
33859
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120000
gel filtration
117000
-
gel filtration
33000
-
4 * 33000, SDS-PAGE
33858
-
4 * 33858, calculation from nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
homotetramer
-
-
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallizations are performed using the hanging-drop vapour-diffusion method at 19.9°C, structures of crystals soaked with the substrate uric acid, the inhibitor 8-azaxanthin and allantoin are determined at 1.9-2.2 A resolution, 2 homotetramers comprise the asymmetric crystallographic unit, each subunit contains 2 T-fold domains of topology, which are usually found in purine- and pterin-binding enzymes, the uric acid substrate is bound tightly to the enzyme by interactions with Arg180, Leu222 and Gln223 from one subunit and with Thr67 and sp68 of the neighbouring subunit in the tetramer
mutant enzyme K12C/E286C, sitting drop vapor diffusion method, using 12% (w/v) polyethylene glycol 3350 and 0.1 M sodium malonate (pH 5.0)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K12C/E286C
the mutations introduce disulfide bonds between the subunits and markedly increase the melting temperature (from 61 to 75°C) of the enzyme compared with wild type
S296C/C302S
the mutations introduce disulfide bonds between the subunits and markedly increase the melting temperature (from 61 to 70°C) of the enzyme compared with wild type
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5 - 11
-
stable
659535
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
61
melting temperature
60
-
10 min, stable
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by anion exchange and hydropbobic interaction chromatography
nickel resin column chromatography and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a plasmid containing the AgUOX gene is introduced into the expression host cell Escherichia coli DH1
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli, Escherichia coli harboring pUOD1 produces 20fold higher uricase than the original Arthrobacter strain, even without an inducer
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Suzuki, K.; Sakasegawa, S.I.; Misaki, H.; Sugiyama, M.
Molecular cloning and expression of uricase gene from Arthrobacter globiformis in Escherichia coli and characterization of the gene product
J. Biosci. Bioeng.
98
153-158
2004
Arthrobacter globiformis, Arthrobacter globiformis FERM BP-360
Manually annotated by BRENDA team
Kim, W.K.; Patterson, P.H.
Production of an egg yolk antibody specific to microbial uricase and its inhibitory effects on uricase activity
Poult. Sci.
82
1554-1558
2003
Arthrobacter globiformis
Manually annotated by BRENDA team
Juan, E.; Hoque, M.; Shimizu, S.; Hossain, M.; Yamamoto, T.; Imamura, S.; Suzuki, K.; Tsunoda, M.; Amano, H.; Sekiguchi, T.; Takenaka, A.
Structures of Arthrobacter globiformis urate oxidase-ligand complexes
ACTA CRYSTALLOGR. SECT. D
64
815-822
2008
Arthrobacter globiformis (D0VWQ1), Arthrobacter globiformis
Manually annotated by BRENDA team
Shi, Y.; Wang, T.; Zhou, X.E.; Liu, Q.F.; Jiang, Y.; Xu, H.E.
Structure-based design of a hyperthermostable AgUricase for hyperuricemia and gout therapy
Acta Pharmacol. Sin.
40
1364-1372
2019
Arthrobacter globiformis (D0VWQ1), Arthrobacter globiformis
Manually annotated by BRENDA team
Gruia, F.; Parupudi, A.; Baca, M.; Ward, C.; Nyborg, A.; Remmele, R.L.; Bee, J.S.
Impact of mutations on the higher order structure and activity of a recombinant uricase
J. Pharm. Sci.
106
1018-1024
2017
Arthrobacter globiformis
Manually annotated by BRENDA team