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Information on EC 1.14.12.15 - terephthalate 1,2-dioxygenase
for references in articles please use BRENDA:EC1.14.12.15
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.12 With NADH or NADPH as one donor, and incorporation of two atoms of oxygen into the other donor
1.14.12.15 terephthalate 1,2-dioxygenase
IUBMB Comments
Has been shown to contain a Rieske [2Fe-2S] cluster
The enzyme appears in viruses and cellular organisms
- 1.14.12.15
- comamonas
- testosteroni
- protocatechuate
-
rieske
-
ring-hydroxylating
Reaction Schemes
showSynonyms
tpado, terdos, terephthalate 1,2-dioxygenase, tpa 1,2-dioxygenase, ter dioxygenase system, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,4-Dicarboxybenzoate 1,2-dioxygenase
-
-
-
-
Benzene-1,4-dicarboxylate 1,2-dioxygenase
-
-
-
-
Oxygenase, terephthalate, 1,2-di
-
-
-
-
TER dioxygenase system
-
-
-
-
TERDOS
-
-
-
-
TPA 1,2-dioxygenase
TPADO
TPADO
-
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
-
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
-
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
-
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
terephthalate degradation
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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
LITERATURE
COMMENTARY
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)+
-
Substrates: NADPH is the preferred electron donor compared to NADH
Products: -
Products: -
?
terephthalate + NAD(P)H + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD(P)+
-
Substrates: TPADO is specific for terephthalate
Products: -
Products: -
?
terephthalate + NAD(P)H + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD(P)+
-
Substrates: NADPH is the preferred electron donor compared to NADH
Products: -
Products: -
?
terephthalate + NAD(P)H + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD(P)+
-
Substrates: TPADO is specific for terephthalate
Products: -
Products: -
?
terephthalate + NAD(P)H + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD(P)+
-
Substrates: NADPH is the preferred electron donor compared to NADH
Products: -
Products: -
?
terephthalate + NAD(P)H + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD(P)+
-
Substrates: NADPH is the preferred electron donor compared to NADH
Products: -
Products: -
?
terephthalate + NADH + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD+
-
Substrates: -
Products: -
Products: -
?
terephthalate + NADH + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD+
-
Substrates: -
Products: -
Products: -
?
terephthalate + NADH + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD+
-
Substrates: -
Products: -
Products: -
?
terephthalate + NADH + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD+
-
Substrates: -
Products: -
Products: -
?
terephthalate + NADH + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD+
Substrates: -
Products: -
Products: -
?
terephthalate + NADH + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD+
Substrates: -
Products: -
Products: -
?
terephthalate + NADH + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD+
-
Substrates: -
Products: -
Products: -
?
terephthalate + NADH + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD+
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: phthalate, isophthalate, benzoate, p-hydroxybenzoate, biphenyl, benzene, and toluene are no substrates of TPADO
Products: -
Products: -
?
additional information
?
-
-
Substrates: does not catalyze phthalate, isophthalate, hydrobenzoate, protocatechuate, gallate, syringate, vanillate, benzoate, and 4-chlorobenzoate
Products: -
Products: -
?
additional information
?
-
-
Substrates: phthalate, isophthalate, benzoate, p-hydroxybenzoate, biphenyl, benzene, and toluene are no substrates of TPADO
Products: -
Products: -
?
additional information
?
-
-
Substrates: does not catalyze phthalate, isophthalate, hydrobenzoate, protocatechuate, gallate, syringate, vanillate, benzoate, and 4-chlorobenzoate
Products: -
Products: -
?
additional information
?
-
-
Substrates: phthalate, isophthalate, benzoate, p-hydroxybenzoate, biphenyl, benzene, and toluene are no substrates of TPADO
Products: -
Products: -
?
additional information
?
-
-
Substrates: phthalate, isophthalate, benzoate, p-hydroxybenzoate, biphenyl, benzene, and toluene are no substrates of TPADO
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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+
Substrates: -
Products: -
Products: -
?
terephthalate + NADH + O2 + H+
(1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate + NAD+
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
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+
-
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
-
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
-
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
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
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
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). TPDR1_COMSP
Comamonas sp
336
0
36342
Swiss-Prot
other Location (Reliability: 1)
TPDB1_COMSP
Comamonas sp
154
0
17231
Swiss-Prot
other Location (Reliability: 3)
TPDA1_COMSP
Comamonas sp
413
0
46303
Swiss-Prot
Secretory Pathway (Reliability: 1)
A0AA42PZX7_9BURK
336
0
36342
TrEMBL
Secretory Pathway (Reliability: 1)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
126000
-
oxygenase component of the TER dioxygenase system, gel filtration
17000
17236
-
2 * 48000, SDS-PAGE, TphA2II + 2 * 17000, SDS-PAGE, TphA3II. 2 * 48763, sequence analysis, TphA2II + 2 * 17236, sequence analysis, TphA3II
18000
-
2 * 49000, alpha, + 2 * 18000, beta, oxygenase component of the TER dioxygenase system, SDS-PAGE
48000
-
2 * 48000, SDS-PAGE, TphA2II + 2 * 17000, SDS-PAGE, TphA3II. 2 * 48763, sequence analysis, TphA2II + 2 * 17236, sequence analysis, TphA3II
48763
-
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
-
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
-
tetramer
-
2 * 49000, alpha, + 2 * 18000, beta, oxygenase component of the TER dioxygenase system, SDS-PAGE
tetramer
-
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
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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 sp. E6, Comamonas testosteroni, Comamonas testosteroni IAM 1152
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. (in: high G+C Gram-positive bacteria), Rhodococcus sp. (in: high G+C Gram-positive bacteria) 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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