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Literature summary extracted from

  • Henderson, K.L.; Le, V.H.; Lewis, E.A.; Emerson, J.P.
    Exploring substrate binding in homoprotocatechuate 2,3-dioxygenase using isothermal titration calorimetry (2012), J. Biol. Inorg. Chem., 17, 991-994.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.11.15 3,4-dihydroxyphenylacetate + O2 Brevibacterium fuscum
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 2-hydroxy-5-carboxymethylmuconate semialdehyde
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 ?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.15 Brevibacterium fuscum
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.15 3,4-dihydroxyphenylacetate + O2
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 Brevibacterium fuscum 2-hydroxy-5-carboxymethylmuconate semialdehyde
-
 ?
1.13.11.15 4-nitrocatechol + O2 not the native substrate for HPCD, it is cleaved in a similar fashion as the natural substrate, homoprotocatechuate, 4-nitrocatechol exhibits characteristic visible absorption bands that are sensitive to its ionization and oxidation states, suitable for spectral substrate binding and reaction mechanism analysis Brevibacterium fuscum ?
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 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.11.15 homoprotocatechuate 2,3-dioxygenase
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 Brevibacterium fuscum
1.13.11.15 HPCD
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 Brevibacterium fuscum

General Information

EC Number General Information Comment Organism
1.13.11.15 additional information proposed mechanism for homoprotocatechuate binding to homoprotocatechuate 2,3-dioxygenase, substrate binding structure and thermodynamics, isothermal titration calorimetry analysis, overview Brevibacterium fuscum