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
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testosteroni
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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
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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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Activating Compound
Activating Compound on EC 1.13.11.8 - protocatechuate 4,5-dioxygenase
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heteroallosteric activation of LigAB by vanillin at an allosteric binding site in LigAB, regulatory feed-forward activation mechanism, kinetics, overview. Vanillin is the pre-pre-substrate of LigAB. Enhancement by vanillin is specific to protocatechuate. Glu86b is directly involved in a hydrogen bond network through the carboxylate with Ndelta of His127b, believed to be the catalytic base that performs the initial substrate deprotonation. The His127b methylene also contributes a small fraction to the identified allosteric binding pocket
Vanillin
like the wild-type enzyme, F103T and F103V alpha-subunit point mutants also exhibit allosteric activation for the dioxygenation of protocatechuate and gallate, respectively
allosteric rate enhancement in the presence of non-substrate protocatechuate-like aldehydes such as vanillin
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additional information
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allosteric rate enhancement in the presence of non-substrate protocatechuate-like aldehydes such as vanillin
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additional information
impact of alpha-subunit Phe103alpha mutations on allosteric activation of alternate substrate dioxygenation by vanillin compared to the wild-type enzyme, overview
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