1.13.11.8: protocatechuate 4,5-dioxygenase
This is an abbreviated version!
For detailed information about protocatechuate 4,5-dioxygenase, go to the full flat file.
Word Map on EC 1.13.11.8
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1.13.11.8
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paucimobilis
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extradiol
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sphingomonas
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vanillate
-
testosteroni
-
2-pyrone-4,6-dicarboxylate
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3,4-dioxygenase
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3-o-methylgallate
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4,5-cleavage
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comamonas
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meta-cleavage
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o-demethylase
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4-oxalomesaconate
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sphingobium
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tetrahydrofolate-dependent
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ring-cleavage
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nishikawa
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extradiol-type
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ochraceae
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katayama
-
2,3-dihydroxybiphenyl
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biofuel production
- 1.13.11.8
- paucimobilis
-
extradiol
- sphingomonas
- vanillate
- testosteroni
- 2-pyrone-4,6-dicarboxylate
-
3,4-dioxygenase
- 3-o-methylgallate
-
4,5-cleavage
- comamonas
-
meta-cleavage
- o-demethylase
- 4-oxalomesaconate
- sphingobium
-
tetrahydrofolate-dependent
-
ring-cleavage
-
nishikawa
-
extradiol-type
- ochraceae
-
katayama
- 2,3-dihydroxybiphenyl
- biofuel production
Reaction
Synonyms
LigAB, PCA 4,5-dioxygenase, PcaA, PCD 4,5, PCD4,5, PmdAB, protocatechuate 4,5-oxygenase, protocatechuic 4,5-dioxygenase, protocatechuic 4,5-oxygenase
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Reference
Reference on EC 1.13.11.8 - protocatechuate 4,5-dioxygenase
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Trippett, S.; Dagley, S.; Stopher, D.A.
Bacterial oxidation of protocatechuic acid
Biochem. J.
76
9P
1960
Pseudomonas sp.
-
Arciero, D.M.; Orville, A.M.; Lipscomb, J.D.
Protocatechuate 4,5-dioxygenase from Pseudomonas testosteroni
Methods Enzymol.
188
89-95
1990
Comamonas testosteroni, Comamonas testosteroni Pt-L5 / ATCC 49249
Zabinski, R.; Munck, E.; Champion, P.M.; Wood, J.M.
Kinetic and Mossbauer studies on the mechanism of protocatechuic acid 4,5-oxygenase
Biochemistry
11
3212-3219
1972
Comamonas testosteroni
Arciero, D.M.; Lipscomb, J.D.
Binding of 17O-labeled substrate and inhibitors to protocatechuate 4,5-dioxygenase-nitrosyl complex. Evidence for direct substrate binding to the active site Fe2+ of extradiol dioxygenases
J. Biol. Chem.
261
2170-2178
1986
Comamonas testosteroni, Comamonas testosteroni Pt-L5 / ATCC 49249
Arciero, D.M.; Orville, A.M.; Lipscomb, J.D.
Water and nitric oxide binding by protocatechuate 4,5-dioxygenase and catechol 2,3-dioxygenase. Evidence for binding of exogenous ligands to the active site Fe2+ of extradiol dioxygenases
J. Biol. Chem.
260
14035-14044
1985
Comamonas testosteroni, Comamonas testosteroni Pt-L5 / ATCC 49249
Arciero, D.M.; Lipscomb, J.D.; Huynh, B.H.; Kent, T.A.; Munck, E.
EPR and Mossbauer studies of protocatechuate 4,5-dioxygenase. Characterization of a new Fe2+ environment
J. Biol. Chem.
258
14981-14991
1983
Comamonas testosteroni
Chen, Y.P.; Lovell, C.R.
Purification and properties of a homodimeric protocatechuate 4,5-dioxygenase from Rhizobium leguminosarum
Arch. Microbiol.
161
191-195
1994
Rhizobium leguminosarum
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Sugimoto, K.; Senda, T.; Aoshima, H.; Masai, E.; Fukuda, M.; Mitsui, Y.
Crystal structure of an aromatic ring opening dioxygenase LigAB, a protocatechuate 4,5-dioxygenase, under aerobic conditions
Structure
7
953-965
1999
Sphingomonas paucimobilis, Sphingomonas paucimobilis SYK-6
Mampel, J.; Providenti, M.A.; Cook, A.M.
Protocatechuate 4,5-dioxygenase from Comamonas testosteroni T-2: biochemical and molecular properties of a new subgroup within class III of extradiol dioxygenases
Arch. Microbiol.
183
130-139
2005
Comamonas testosteroni (Q8RNX9), Comamonas testosteroni (Q8RNY0), Comamonas testosteroni, Comamonas testosteroni T-2 (Q8RNX9), Comamonas testosteroni T-2 (Q8RNY0), Comamonas testosteroni T-2
Yun, S.H.; Yun, C.Y.; Kim, S.I.
Characterization of protocatechuate 4,5-dioxygenase induced from p-hydroxybenzoate-cultured Pseudomonas sp. K82
J. Microbiol.
42
152-155
2004
Pseudomonas sp. K82
Yoon, Y.; Park, S.; Leem, S.; Kim, S.I.
Cloning of p-hydroxybenzoate degradation genes and the overexpression of protocatechuate 4,5-dioxygenase from Pseudomonas sp. K82
J. Microbiol. Biotechnol.
16
1995-1999
2006
Pseudomonas sp. (Q1WCM6), Pseudomonas sp. (Q1WCM7)
-
Kasai, D.; Masai, E.; Katayama, Y.; Fukuda, M.
Degradation of 3-O-methylgallate in Sphingomonas paucimobilis SYK-6 by pathways involving protocatechuate 4,5-dioxygenase
FEMS Microbiol. Lett.
274
323-328
2007
Sphingomonas paucimobilis, Sphingomonas paucimobilis SYK-6
Kamimura, N.; Aoyama, T.; Yoshida, R.; Takahashi, K.; Kasai, D.; Abe, T.; Mase, K.; Katayama, Y.; Fukuda, M.; Masai, E.
Characterization of the protocatechuate 4,5-cleavage pathway operon in Comamonas sp. strain E6 and discovery of a novel pathway gene
Appl. Environ. Microbiol.
76
8093-8101
2010
Comamonas sp., Comamonas sp. E6
Kersten, P.J.; Dagley, S.; Whittaker, J.W.; Arciero, D.M.; Lipscomb, J.D.
2-pyrone-4,6-dicarboxylic acid, a catabolite of gallic acids in Pseudomonas species
J. Bacteriol.
152
1154-1162
1982
Brevibacterium fuscum
Wojcieszynska, D.; Guzik, U.; Gren, I.; Perkosz, M.; Hupert-Kocurek, K.
Induction of aromatic ring: cleavage dioxygenases in Stenotrophomonas maltophilia strain KB2 in cometabolic systems
World J. Microbiol. Biotechnol.
27
805-811
2011
no activity in Stenotrophomonas maltophilia, no activity in Stenotrophomonas maltophilia KB2
Barry, K.P.; Ngu, A.; Cohn, E.F.; Cote, J.M.; Burroughs, A.M.; Gerbino, J.P.; Taylor, E.A.
Exploring allosteric activation of LigAB from Sphingobium sp. strain SYK-6 through kinetics, mutagenesis and computational studies
Arch. Biochem. Biophys.
567
35-45
2015
Sphingobium sp. (G2IQQ4 AND G2IQQ3), Sphingobium sp.
Kamimura, N.; Masai, E.
The protocatechuate 4,5-cleavage pathway overview and new findings
Biodegr. Bacteria
2014
207-226
2014
Comamonas sp., Sphingobium sp.
-
Barry, K.; Cohn, E.; Ngu, A.; Taylor, E.
Improving alternate lignin catabolite utilization of LigAB from Sphingobium sp. strain SYK-6 through site directed mutagenesis
Process Biochem.
50
1634-1639
2015
Sphingobium sp. (G2IQQ4 AND G2IQQ3)
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Tsagogiannis, E.; Vandera, E.; Primikyri, A.; Asimakoula, S.; Tzakos, A.G.; Gerothanassis, I.P.; Koukkou, A.I.
Characterization of protocatechuate 4,5-dioxygenase from Pseudarthrobacter phenanthrenivorans Sphe3 and in situ reaction monitoring in the NMR tube
Int. J. Mol. Sci.
22
9647
2021
Pseudarthrobacter phenanthrenivorans (F0MCP7), Pseudarthrobacter phenanthrenivorans Sphe3 (F0MCP7), Pseudarthrobacter phenanthrenivorans Sphe3
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