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Information on EC 1.13.11.4 - gentisate 1,2-dioxygenase and Organism(s) Ruegeria pomeroyi and UniProt Accession Q5LLB1

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IUBMB Comments
Requires Fe2+.
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This record set is specific for:
Ruegeria pomeroyi
UNIPROT: Q5LLB1
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The taxonomic range for the selected organisms is: Ruegeria pomeroyi
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
gentisate 1,2-dioxygenase, salicylate 1,2-dioxygenase, gentisate dioxygenase, gdosp, gdo-ii, gentisate-1,2-dioxygenase, gentisate oxygenase, gentisate:oxygen 1,2-oxidoreductase (decyclizing), p25x gentisate 1,2-dioxygenase, p35x gentisate 1,2-dioxygenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2,5-dihydroxybenzoate dioxygenase
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-
-
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gentisate dioxygenase
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-
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gentisate oxygenase
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-
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gentisic acid oxidase
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-
-
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oxygenase, gentisate 1,2-di-
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-
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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-
SYSTEMATIC NAME
IUBMB Comments
gentisate:oxygen 1,2-oxidoreductase (decyclizing)
Requires Fe2+.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-48-5
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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
2,5-dihydroxybenzoate + O2
maleylpyruvate
show the reaction diagram
2,5-dihydroxybenzoate + O2
maleylpyruvate
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
2,5-dihydroxybenzoate + O2
maleylpyruvate
show the reaction diagram
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-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
contains ferrous iron
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
2 mM, complete inhibition
EDTA
100 mM, complete inhibition
Hg2+
2 mM, complete inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012
2,5-Dihydroxybenzoate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.6 - 4.8
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
DSS-3
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
132000
gel filtration
45000
3 * 45000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
3 * 45000, SDS-PAGE
homotetramer
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-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure at 2.8 A resolution, hanging drop vapor diffusion crystallization at 16°C. The crystal form belongs to the R32 space group, with two protein molecules (named as A and B) per asymmetric unit and 45% solvent content
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D175N
inactive mutant enzyme
D225N
activity is comparable to wild-type activity
E47Q
activity is comparable to wild-type activity
H119A/H121A
despite its wild-type like structural propertie, the mutant shows extremely low gentisate 1,2-dioxygenase activity
H290A/H292A
mutant can not be expressed in a soluble form
L39T
activity is comparable to wild-type activity
P253_Y254del
mutation reduces the activity to 30%
Q108E
inactive mutant enzyme
Q108E/D175N
activity is near zero
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
protein unfolds and loses its secondary structures above
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 1 week, purified enzyme loses 51% of its initial activity
-70°C, 1 week, purified enzyme loses 30% of its initial activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Liu, D.; Zhu, T.; Fan, L.; Quan, J.; Guo, H.; Ni, J.
Identification of a novel gentisate 1,2-dioxygenase from Silicibacter pomeroyi
Biotechnol. Lett.
29
1529-1535
2007
Ruegeria pomeroyi (Q5LLB1), Ruegeria pomeroyi
Manually annotated by BRENDA team
Chen, J.; Li, W.; Wang, M.; Zhu, G.; Liu, D.; Sun, F.; Hao, N.; Li, X.; Rao, Z.; Zhang, X.C.
Crystal structure and mutagenic analysis of GDOsp, a gentisate 1,2-dioxygenase from Silicibacter pomeroyi
Protein Sci.
17
1362-1373
2008
Ruegeria pomeroyi (Q5LLB1), Ruegeria pomeroyi
Manually annotated by BRENDA team
Eppinger, E.; Ferraroni, M.; Buerger, S.; Steimer, L.; Peng, G.; Briganti, F.; Stolz, A.
Function of different amino acid residues in the reaction mechanism of gentisate 1,2-dioxygenases deduced from the analysis of mutants of the salicylate 1,2-dioxygenase from Pseudaminobacter salicylatoxidans
Biochim. Biophys. Acta
1854
1425-1437
2015
Ruegeria pomeroyi
Manually annotated by BRENDA team