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Literature summary for 1.13.11.15 extracted from

  • Mbughuni, M.M.; Chakrabarti, M.; Hayden, J.A.; Meier, K.K.; Dalluge, J.J.; Hendrich, M.P.; Muenck, E.; Lipscomb, J.D.
    Oxy intermediates of homoprotocatechuate 2,3-dioxygenase: facile electron transfer between substrates (2011), Biochemistry, 50, 10262-10274.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.13.11.15

Protein Variants

Protein Variants Comment Organism
H200N site-directed mutagenesis, catalytic reaction intermediate formation in the mutant differs from the wild-type enzyme, Mössbauer spectral analysis, overview Brevibacterium fuscum

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+
-
 Brevibacterium fuscum
Fe2+ FeHPCD, substrates homoprotocatechuate and O2 bind to the Fe2+ of homoprotocatechuate 2,3-dioxygenase in adjacent coordination sites Brevibacterium fuscum
Mn2+ MnHPCD Brevibacterium fuscum
additional information the enzyme is fully functional using metals with a redox potential range spanning 1.15 V. Recombinant extradiol dioxygenase homoprotocatechuate 2,3-dioxygenase functions with the same kcat, and kcat/KmO2 values within error when the Fe2+ is replaced by Mn2+. It exhibits even higher kcat and KmO2 values when Co2+ is substituted Brevibacterium fuscum

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Brevibacterium fuscum
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3,4-dihydroxyphenylacetate + O2
-
 Brevibacterium fuscum 2-hydroxy-5-carboxymethylmuconate semialdehyde
-
 ?
3,4-dihydroxyphenylacetate + O2 substrates homoprotocatechuate and O2 bind to the Fe2+ of homoprotocatechuate 2,3-dioxygenase in adjacent coordination sites. Transfer of an electron(s) from 3,4-dihydroxyphenylacetate to O2 via the iron is proposed to activate the substrates for reaction with each other to initiate aromatic ring cleavage. Oxygen is bound as a (hydro)peroxo ligand. At least four intermediates form following addition of O2 with a pre-formed enzyme-substrate complex, different intermediate formation in mutant H200N, Mössbauer spectral analysis, overview Brevibacterium fuscum 2-hydroxy-5-carboxymethylmuconate semialdehyde
-
 ?

Synonyms

Synonyms Comment Organism
FeHPCD
-
 Brevibacterium fuscum
homoprotocatechuate 2,3-dioxygenase
-
 Brevibacterium fuscum
MnHPCD
-
 Brevibacterium fuscum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 assay at room temperature Brevibacterium fuscum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Brevibacterium fuscum