Information on EC 1.97.1.2 - pyrogallol hydroxytransferase

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The expected taxonomic range for this enzyme is: Pelobacter

EC NUMBER
COMMENTARY hide
1.97.1.2
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RECOMMENDED NAME
GeneOntology No.
pyrogallol hydroxytransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
1,2,3,5-tetrahydroxybenzene + 1,2,3-trihydroxybenzene = 1,3,5-trihydroxybenzene + 1,2,3,5-tetrahydroxybenzene
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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-
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reduction
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-
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transhydroxylation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Aminobenzoate degradation
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gallate degradation III (anaerobic)
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
1,2,3,5-tetrahydroxybenzene:1,2,3-trihydroxybenzene hydroxytransferase
1,2,3,5-Tetrahydroxybenzene acts as a co-substrate for the conversion of pyrogallol into phloroglucinol, and for a number of similar isomerizations. The enzyme is provisionally listed here, but might be considered as the basis for a new class in the transferases, analogous to the aminotransferases.
CAS REGISTRY NUMBER
COMMENTARY hide
125978-84-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain MaGal 2
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,2,3,5-tetrahydroxybenzene + 1,2,3,5-tetrahydroxybenzene
phloroglucinol + pentahydroxybenzene
show the reaction diagram
1,2,3,5-tetrahydroxybenzene + 1,2,3-trihydroxybenzene
1,3,5-trihydroxybenzene + 1,2,3,5-tetrahydroxybenzene
show the reaction diagram
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2,4,6,3’,4’,5’-hexahydroxydiphenyl ether and 3,4,5,3’,4’,5’-hexahydroxydiphenyl ether can substitute for the cocatalyst 1,2,3,5-tetrahydroxybenzene in vitro. This indicates that the diphenyl ethers can intrude into the active site and initiate the catalytic cycle
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?
1,2,3,5-tetrahydroxybenzene + hydroxyhydroquinone
phloroglucinol + 1,2,4,5-tetrahydroxybenzene
show the reaction diagram
1,2,3,5-tetrahydroxybenzene + pyrogallol
?
show the reaction diagram
1,2,3,5-tetrahydroxybenzene + pyrogallol
phloroglucinol + 1,2,3,5-tetrahydroxybenzene
show the reaction diagram
1,2,3,5-tetrahydroxybenzene + resorcinol
phloroglucinol + hydroxyhydroquinone
show the reaction diagram
1,2,4,5-tetrahydroxybenzene + pyrogallol
hydroxyhydroquinone + 1,2,3,5-tetrahydroxybenzene
show the reaction diagram
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?
hydroxyhydroquinone + hydroxyhydroquinone
resorcinol + 1,2,4,5-tetrahydroxybenzene
show the reaction diagram
hydroxyhydroquinone + pyrogallol
resorcinol + 1,2,3,5-tetrahydroxybenzene
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
1,2,3,5-tetrahydroxybenzene + pyrogallol
?
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
molybdenum cofactor
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Molybdenum
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molybdopterin-containing enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
resorcinol
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complete inhibition of the reaction of hydroxyhydroquinone with itself
additional information
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oxygen does not inactivate, but the assay requires strict anaerobiosis due to the instability of the substrates and products
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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no activation by reducing agents
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.71
1,2,3,5-Tetrahydroxybenzene
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.34
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1,2,3,5-tetrahydroxybenzene + hydroxyhydroquinone
0.4
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1,2,4,5-tetrahydroxybenzene
additional information
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oxides tested as cosubstrates
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
130500
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excluding cofactors, calculation from amino acid sequence
133000
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mass spectrometry
160000
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polar plot of self-rotation function
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pyrogallol-phloroglucinol transhydroxylase complex and 1,2,4-trihydroxybenzene pyrogallol-phloroglucinol transhydroxylase complex. Crystal structure of the enzyme in the reduced Mo(IV) state, which is solved by single anomalous diffraction technique
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxides replace the physiological cosubstrate, p.e. pyridine N-oxide, 2-hydroxypyridine N-oxide, DMSO and tetramethylene sulfoxide
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437679
oxygen does not inactivate, but the assay requires strict anaerobiosis because of the instability of the substrates and products
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437674
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli strain BL21 and M15
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