1.13.11.4: gentisate 1,2-dioxygenase
This is an abbreviated version!
For detailed information about gentisate 1,2-dioxygenase, go to the full flat file.
Word Map on EC 1.13.11.4
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1.13.11.4
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maleylpyruvate
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protocatechuate
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3-hydroxybenzoate
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pseudaminobacter
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salicylatoxidans
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1-hydroxy-2-naphthoate
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3,4-dioxygenase
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monohydroxylated
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fumarylpyruvate
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isofunctional
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5-hydroxylase
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ring-fission
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ring-cleaving
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extradiol
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bicupins
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nocardioides
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acidovorans
- 1.13.11.4
- maleylpyruvate
- protocatechuate
- 3-hydroxybenzoate
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pseudaminobacter
- salicylatoxidans
- 1-hydroxy-2-naphthoate
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3,4-dioxygenase
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monohydroxylated
- fumarylpyruvate
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isofunctional
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5-hydroxylase
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ring-fission
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ring-cleaving
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extradiol
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bicupins
- nocardioides
- acidovorans
Reaction
Synonyms
2,5-dihydroxybenzoate dioxygenase, DsmD, EC 1.13.1.4, EC 1.99.2.4, eGDO, GDO, GDO-II, gdoA, GDOsp, GenH, gentisate dioxygenase, gentisate oxygenase, gentisate-1,2-dioxygenase, gentisic acid oxidase, gtdA-2, hbzE, Nagl1, Nagl2, Nagl3, NarI, oxygenase, gentisate 1,2-di-, P25X gentisate 1,2-dioxygenase, P35X gentisate 1,2-dioxygenase, salicylate 1,2-dioxygenase, SDO
ECTree
1.13.11.4 gentisate 1,2-dioxygenaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.13.11.4 - gentisate 1,2-dioxygenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A112D
the mutant gains the ability to oxidize salicylate and several other monohydroxylated substrates
A112G
A112I
the mutant gains the ability to oxidize salicylate and several other monohydroxylated substrates
A112S
the mutant gains the ability to oxidize salicylate and several other monohydroxylated substrates
A112D
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the mutant gains the ability to oxidize salicylate and several other monohydroxylated substrates
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A112G
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the mutant gains the ability to oxidize salicylate and several other monohydroxylated substrates
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A112I
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the mutant gains the ability to oxidize salicylate and several other monohydroxylated substrates
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A112S
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the mutant gains the ability to oxidize salicylate and several other monohydroxylated substrates
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G106A
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site-directed mutagenesis, in contrast to the wild-type enzyme, mutant G106A oxidizes only gentisate, while 1-hydroxy-2-naphthoate and salicylate are not converted. The mutant shows slightly decreased activity with salicylate, but shows a higher affinity to this substratecompared to the wild-type. Salicylate is coordinated in the G106A variant with the catalytically active Fe(II) ion in an unusual and unproductive manner because of the inability of salicylate to displace a hydrogen bond that is formed between Trp104 and Asp174 in the G106A variant
G106A
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site-directed mutagenesis, in contrast to the wild-type enzyme, mutant G106A oxidizes only gentisate, while 1-hydroxy-2-naphthoate and salicylate are not converted. The mutant shows slightly decreased activity with salicylate, but shows a higher affinity to this substratecompared to the wild-type. Salicylate is coordinated in the G106A variant with the catalytically active Fe(II) ion in an unusual and unproductive manner because of the inability of salicylate to displace a hydrogen bond that is formed between Trp104 and Asp174 in the G106A variant
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Y181F
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mutant demonstrates 4-, 3-, 6-, and 16fold increase in relative activity towards 2,5-dihydroxybenzoate, 3-fluoro-, 4-methyl-, and 3-methylgentisate, respectively, and shows 464% relative activity compared to the wild type enzyme for 2,5-dihydroxybenzoate
Y181F
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mutant demonstrates 4-, 3-, 6-, and 16fold increase in relative activity towards 2,5-dihydroxybenzoate, 3-fluoro-, 4-methyl-, and 3-methylgentisate, respectively, and shows 464% relative activity compared to the wild type enzyme for 2,5-dihydroxybenzoate
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H119A/H121A
despite its wild-type like structural propertie, the mutant shows extremely low gentisate 1,2-dioxygenase activity
additional information
A112G
the mutant gains the ability to oxidize salicylate and several other monohydroxylated substrates
A112G
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mutation does not alter the nature of the Fe-substrate-O2 ternary complex
additional information
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construction of individual knockout mutants of all three nagI genes via 2 bp unmarked gene deletion mutagenesis, all three nagI knockout mutants still contain stop codons within their nagI genes. Mutant CJ2DELTAnagI3 shows severely diminished GDO activity and grows slowest on aromatic substrates
additional information
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double mutant Phe3Leu, Val334Ala, doubled enzymatic activity, mutants in conserved core regions with less activity
