Information on EC 4.1.1.103 - gamma-resorcylate decarboxylase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.1.1.103
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RECOMMENDED NAME
GeneOntology No.
gamma-resorcylate decarboxylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2,6-dihydroxybenzoate = 1,3-dihydroxybenzene + CO2
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Benzoate degradation
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gamma-resorcylate degradation I
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gamma-resorcylate degradation II
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
2,6-dihydroxybenzoate carboxy-lyase
The enzyme, characterized from several bacterial strains, is involved in the degradation of gamma-resorcylate. It contains a zinc ion and a water molecule at the active site. The reaction is reversible, but equilibrium greatly favors the decarboxylation reaction.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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expression of the tsdA gene confers gamma-resorcylate decarboxylase activity on Escherichia coli. Transcription of the tsdBADC and tsdTX operons required for gamma-resorcylate catabolism is induced during growth on gamma-resorcylate. Inactivation of tsdR derepresses transcription of the tsdBADC and tsdTX operons in the absence of gamma-resorcylate
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,2-dihydroxybenzen + CO2
2,3-dihydroxybenzoate
show the reaction diagram
1,3-dihydroxybenzene + CO2
2,6-dihydroxybenzoate
show the reaction diagram
2,3-dihydroxybenzoate
1,2-dihydroxybenzene + CO2
show the reaction diagram
2,3-Dihydroxybenzoate
Catechol + CO2
show the reaction diagram
2,6-dihydroxybenzoate
1,3-dihydroxybenzene + CO2
show the reaction diagram
catechol + CO2
2,3-dihydroxybenzoate
show the reaction diagram
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r
phenol + + CO2
4-hydroxybenzoate
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1,3-dihydroxybenzene + CO2
2,6-dihydroxybenzoate
show the reaction diagram
2,3-Dihydroxybenzoate
Catechol + CO2
show the reaction diagram
2,6-dihydroxybenzoate
1,3-dihydroxybenzene + CO2
show the reaction diagram
catechol + CO2
2,3-dihydroxybenzoate
show the reaction diagram
Q60FX6
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
1 mM, 132% of initial activity for decarboxylation reaction, 106% of initial activity for carboxylation reaction
Zn2+
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the native enzyme possesses one Zn2+ ion liganded by Glu8, His10, His164, Asp287, and a water molecule at the active site center
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
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1 mM, 26% loss of activity
diethyl dicarbonate
1 mM, 66% of initial activity for decarboxylation reaction, 62% of initial activity for carboxylation reaction
p-chloromercuribenzoate
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1 mM, 20% loss of activity
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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no activation by pyridoxal 5'-phosphate or thiamin diphosphate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
25.9
1,3-dihydroxybenzene
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pH 7.0, 30C
0.12
2,3-Dihydroxybenzoate
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pH 7.0, 30C
0.08 - 7.1
2,6-dihydroxybenzoate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20
2,6-dihydroxybenzoate
Agrobacterium tumefaciens
Q60FX6
pH 7.0, 40C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.098
1,3-dihydroxybenzene
Rhizobium sp.
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pH 7, 30C
8988
13.4
2,6-dihydroxybenzoate
Rhizobium sp.
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pH 7, 30C
7088
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.57
carboxylation reaction, pH 7.0, 40C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
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more than 80% of maximum activtiy within
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
130000
gel filtration
138000
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gel filtration
151000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structures of native form, the complex with the true substrate (2,6-dihydroxybenzoate), and the complex with 2,3-dihydroxybenzaldehyde at 1.7-, 1.9-, and 1.7-A resolution, respectively. The enzyme exists as a tetramer, and the subunit consists of one (alphabeta)8 triose-phosphate isomerase-barrel domain with three functional linkers and one C-terminal tail. The native enzyme possesses one Zn2+ ion liganded by Glu8, His10, His164, Asp287, and a water molecule at the active site center. The substrate carboxylate takes the place of the water molecule and is coordinated to the Zn2+ ion. The 2-hydroxy group of the substrate is hydrogen-bonded to Asp287, which forms a triad together with His218 and Glu22
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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30 min, 18% loss of activity
70
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30 min, complete loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, potassium phosphate buffer pH 7.0 containing 1 mM dithiothreitol, stable for 7 days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is induced specifically by the addition of gamma-resorcylate to the medium
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the maximum relative mRNA expression level of graF is detected after one h of cultivation when gamma-resorcylate is used as the sole carbon source. The graDAFCBE genes are transcribed as a single mRNA and the transcription of the gene cluster is induced by gamma-resorcylate
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis