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Literature summary for 1.14.14.9 extracted from

  • Chenprakhon, P.; Trisrivirat, D.; Thotsaporn, K.; Sucharitakul, J.; Chaiyen, P.
    Control of C4a-hydroperoxyflavin protonation in the oxygenase component of p-hydroxyphenylacetate-3-hydroxylase (2014), Biochemistry, 53, 4084-4086 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Acinetobacter baumannii

Protein Variants

Protein Variants Comment Organism
H396A mutation of oxygenase component, decrease in hydroxylation efficiency. pKa value is 7.1 compared to 9.8 for wild-type Acinetobacter baumannii
H396N mutation of oxygenase component, decrease in hydroxylation efficiency. pKa value is 9.3 compared to 9.8 for wild-type Acinetobacter baumannii
H396V mutation of oxygenase component, decrease in hydroxylation efficiency. pKa value is 7.3 compared to 9.8 for wild-type Acinetobacter baumannii

Organism

Organism UniProt Comment Textmining
Acinetobacter baumannii Q6Q272 oxygenase component C2
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-hydroxyphenylacetate + NADH + O2
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Acinetobacter baumannii 3,4-dihydroxyphenylacetate + NAD+ + H2O
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additional information proton transfer is not the rate-limiting step in the formation of the C4a-(hydro)peroxyflavin intermediate. Residue His396 may act as an instantaneous proton provider for the proton-coupled electron transfer that occurs before the transition state of C4a-(hydro)peroxyflavin formation Acinetobacter baumannii ?
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