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Information on EC 1.14.12.15 - terephthalate 1,2-dioxygenase
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1.14.12.15 terephthalate 1,2-dioxygenaseIUBMB Comments
Has been shown to contain a Rieske [2Fe-2S] cluster
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The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
tpado, terdos, terephthalate 1,2-dioxygenase, tpa 1,2-dioxygenase, ter dioxygenase system, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,4-Dicarboxybenzoate 1,2-dioxygenase
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-
-
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Benzene-1,4-dicarboxylate 1,2-dioxygenase
-
-
-
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Oxygenase, terephthalate, 1,2-di
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-
-
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TER dioxygenase system
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-
-
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TERDOS
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-
-
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TPA 1,2-dioxygenase
TPADO
TPADO
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TPADO is strongly suggested to be a two-component dioxygenase which consists of the terminal oxygenase component (TphA2 and TphA3) and the reductase component (TphA1)
TPADO
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TPADO is strongly suggested to be a two-component dioxygenase which consists of the terminal oxygenase component (TphA2 and TphA3) and the reductase component (TphA1)
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TPADO
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TPADO is strongly suggested to be a two-component dioxygenase which consists of the terminal oxygenase component (TphA2 and TphA3) and the reductase component (TphA1)
TPADO
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TPADO is strongly suggested to be a two-component dioxygenase which consists of the terminal oxygenase component (TphA2 and TphA3) and the reductase component (TphA1)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
terephthalate + NADH + H+ + O2 = (1R,6S)-dihydroxycyclohexa-2,4-diene-1,4-dicarboxylate + NAD+
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
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reduction
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-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
benzene-1,4-dicarboxylate,NADH:oxygen oxidoreductase (1,2-hydroxylating)
Has been shown to contain a Rieske [2Fe-2S] cluster
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CAS REGISTRY NUMBER
COMMENTARY
162032-76-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
terephthalate + NAD(P)H + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD(P)+
terephthalate + NADH + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD+
terephthalate + NAD(P)H + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD(P)+
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NADPH is the preferred electron donor compared to NADH
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-
?
terephthalate + NAD(P)H + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD(P)+
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TPADO is specific for terephthalate
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-
?
terephthalate + NAD(P)H + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD(P)+
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NADPH is the preferred electron donor compared to NADH
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-
?
terephthalate + NAD(P)H + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD(P)+
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TPADO is specific for terephthalate
-
-
?
terephthalate + NAD(P)H + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD(P)+
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NADPH is the preferred electron donor compared to NADH
-
-
?
terephthalate + NAD(P)H + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD(P)+
-
NADPH is the preferred electron donor compared to NADH
-
-
?
terephthalate + NADH + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD+
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-
-
-
?
terephthalate + NADH + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD+
-
-
-
-
?
terephthalate + NADH + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD+
-
-
-
?
terephthalate + NADH + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD+
-
-
-
?
terephthalate + NADH + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD+
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-
-
?
terephthalate + NADH + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD+
-
-
-
?
terephthalate + NADH + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD+
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-
-
-
?
terephthalate + NADH + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD+
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-
-
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?
additional information
?
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phthalate, isophthalate, benzoate, p-hydroxybenzoate, biphenyl, benzene, and toluene are no substrates of TPADO
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?
additional information
?
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does not catalyze phthalate, isophthalate, hydrobenzoate, protocatechuate, gallate, syringate, vanillate, benzoate, and 4-chlorobenzoate
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?
additional information
?
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phthalate, isophthalate, benzoate, p-hydroxybenzoate, biphenyl, benzene, and toluene are no substrates of TPADO
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?
additional information
?
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does not catalyze phthalate, isophthalate, hydrobenzoate, protocatechuate, gallate, syringate, vanillate, benzoate, and 4-chlorobenzoate
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?
additional information
?
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phthalate, isophthalate, benzoate, p-hydroxybenzoate, biphenyl, benzene, and toluene are no substrates of TPADO
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?
additional information
?
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phthalate, isophthalate, benzoate, p-hydroxybenzoate, biphenyl, benzene, and toluene are no substrates of TPADO
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
terephthalate + NADH + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD+
terephthalate + NADH + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD+
-
-
-
?
terephthalate + NADH + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD+
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
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TphA1II contains 0.7 mol of FAD/mol of protein, it binds one FAD molecule per monomer
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
-
required for activity, inhibited TPADO activity is partially recovered only when Fe2+ is added to the reaction mixture
Fe2+
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required for activity, inhibited TPADO activity is partially recovered only when Fe2+ is added to the reaction mixture
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
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100% inhibition of TphA2IIA3II, Fe2+ restores activity, whereas Co2+, Cu2+, Mg2+, Mn2+, or Zn2+ can not restore activtiy
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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in the presence of 1 mM NADPH, the TPA transformation activity of the crude extract measured in a 1-min reaction is 1.3times higher than that with 1 mM NADH
additional information
-
in the presence of 1 mM NADPH, the TPA transformation activity of the crude extract measured in a 1-min reaction is 1.3times higher than that with 1 mM NADH
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
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TPADO is a two-component enzyme that consists of the termial oxygenase component TphA2IIA3II and the reductase component TphA1II
physiological function
-
TPADO is a two-component enzyme that consists of the termial oxygenase component TphA2IIA3II and the reductase component TphA1II
-
Show AA Sequence and Transmembrane Helices (117 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
126000
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oxygenase component of the TER dioxygenase system, gel filtration
17000
17236
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2 * 48000, SDS-PAGE, TphA2II + 2 * 17000, SDS-PAGE, TphA3II. 2 * 48763, sequence analysis, TphA2II + 2 * 17236, sequence analysis, TphA3II
18000
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2 * 49000, alpha, + 2 * 18000, beta, oxygenase component of the TER dioxygenase system, SDS-PAGE
48000
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2 * 48000, SDS-PAGE, TphA2II + 2 * 17000, SDS-PAGE, TphA3II. 2 * 48763, sequence analysis, TphA2II + 2 * 17236, sequence analysis, TphA3II
48763
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2 * 48000, SDS-PAGE, TphA2II + 2 * 17000, SDS-PAGE, TphA3II. 2 * 48763, sequence analysis, TphA2II + 2 * 17236, sequence analysis, TphA3II
49000
-
2 * 49000, alpha, + 2 * 18000, beta, oxygenase component of the TER dioxygenase system, SDS-PAGE
17000
-
2 * 48000, SDS-PAGE, TphA2II + 2 * 17000, SDS-PAGE, TphA3II. 2 * 48763, sequence analysis, TphA2II + 2 * 17236, sequence analysis, TphA3II
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotetramer
hexamer
monomer
tetramer
heterotetramer
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2 * 48000, SDS-PAGE, TphA2II + 2 * 17000, SDS-PAGE, TphA3II. 2 * 48763, sequence analysis, TphA2II + 2 * 17236, sequence analysis, TphA3II
heterotetramer
-
2 * 48000, SDS-PAGE, TphA2II + 2 * 17000, SDS-PAGE, TphA3II. 2 * 48763, sequence analysis, TphA2II + 2 * 17236, sequence analysis, TphA3II
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tetramer
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2 * 49000, alpha, + 2 * 18000, beta, oxygenase component of the TER dioxygenase system, SDS-PAGE
tetramer
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2 * 49000, alpha, + 2 * 18000, beta, oxygenase component of the TER dioxygenase system, SDS-PAGE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9
-
about 20% of maximum TPADO activity, whereas activity is completely lost at pH 5
702731
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15
-
about 60% of maximum TPADO activity, whereas activity is completely lost at 50°C
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
oxygenase component of the TER dioxygenase system. The reductase component or components cannot be purified
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tag fused tphA1II and His-tag fused tphA2IIA3II genes expressed in Escherichia coli BL21(DE3) harboring pET-16tpa1 and pET-16tpa23 respectively, under the control of the T7 promoter
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schlaefli, H.R.; Weiss, M.A.; Leisinger, T.; Cook, A.M.
Terephthalate 1,2-dioxygenase system from Comamonas testosteroni T-2: purification and some properties of the oxygenase component
J. Bacteriol.
176
6644-6652
1994
Comamonas testosteroni, Comamonas testosteroni T-2
brenda
Shigematsu, T.; Yumihara, K.; Ueda, Y.; Morimura, S.; Kida, K.
Purification and gene cloning of the oxygenase component of the terephthalate 1,2-dioxygenase system from Delftia tsuruhatensis strain T7
FEMS Microbiol. Lett.
220
255-260
2003
Delftia tsuruhatensis (Q8GRC1), Delftia tsuruhatensis, Delftia tsuruhatensis T7 (Q8GRC1)
brenda
Sasoh, M.; Masai, E.; Ishibashi, S.; Hara, H.; Kamimura, N.; Miyauchi, K.; Fukuda, M.
Characterization of the terephthalate degradation genes of Comamonas sp. strain E6
Appl. Environ. Microbiol.
72
1825-1832
2006
Comamonas sp., Comamonas testosteroni, Comamonas testosteroni IAM 1152, Comamonas sp. E6
brenda
Choi, K.Y.; Kim, D.; Sul, W.J.; Chae, J.; Zylstra, G.J.; Kim, Y.M.; Kim, E.
Molecular and biochemical analysis of phthalate and terephthalate degradation by Rhodococcus sp. strain DK17
FEMS Microbiol. Lett.
252
207-213
2005
Rhodococcus sp., Rhodococcus sp. DK17
brenda
Fukuhara, Y.; Kasai, D.; Katayama, Y.; Fukuda, M.; Masai, E.
Enzymatic properties of terephthalate 1,2-dioxygenase of Comamonas sp. strain E6
Biosci. Biotechnol. Biochem.
72
2335-2341
2008
Comamonas sp., Comamonas sp. E6
brenda
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