Kinetics of interaction between substrates/substrate analogs and benzoate 1,2-dioxygenase from benzoate-degrading Rhodococcus opacus 1CP
Language English Country United States Media print-electronic
Document type Journal Article
PubMed
28236176
DOI
10.1007/s12223-017-0505-z
PII: 10.1007/s12223-017-0505-z
Knihovny.cz E-resources
- Keywords
- 2-dioxygenase, Benzoate, Benzoate 1, Inhibitory analysis, R. opacus 1CP, Substrate specificity,
- MeSH
- Bacterial Proteins chemistry genetics metabolism MeSH
- Benzoates chemistry metabolism MeSH
- Biodegradation, Environmental MeSH
- Kinetics MeSH
- Oxygenases chemistry genetics metabolism MeSH
- Rhodococcus chemistry enzymology genetics metabolism MeSH
- Substrate Specificity MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Bacterial Proteins MeSH
- benzoate 1,2-dioxygenase MeSH Browser
- Benzoates MeSH
- Oxygenases MeSH
Benzoate 1,2-dioxygenase (BDO) of Rhodococcus opacus 1CP, which carried out the initial attack on benzoate, was earlier shown to be the enzyme with a narrow substrate specificity. A kinetics of interaction between benzoate 1,2-dioxygenase and substituted benzoates was assessed taking into account the enlarged list of the type of inhibition and using whole cells grown on benzoate. The type of inhibition was determined and the constants of a reaction of BDO with benzoate in the presence of 2-chlorobenzoate (2CBA), 3,5-dichlorobenzoate (3,5DCBA), and 3-methylbenzoate (3MBA) were calculated. For 2CBA and 3MBA, the types of inhibition were classified as biparametrically disсoordinated inhibition and transient inhibition (from activation towards inhibition), respectively. The process of not widely recognized pseudoinhibition of a BDO reaction with benzoate by 3,5DCBA was assessed by the vector method for the representation of enzymatic reactions. Ki value was determined for 2CBA, 3MBA, and 3,5DCBA as 337.5, 870.3, and 14.7 μM, respectively.
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