Kinetics of interaction between substrates/substrate analogs and benzoate 1,2-dioxygenase from benzoate-degrading Rhodococcus opacus 1CP
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články
PubMed
28236176
DOI
10.1007/s12223-017-0505-z
PII: 10.1007/s12223-017-0505-z
Knihovny.cz E-zdroje
- Klíčová slova
- 2-dioxygenase, Benzoate, Benzoate 1, Inhibitory analysis, R. opacus 1CP, Substrate specificity,
- MeSH
- bakteriální proteiny chemie genetika metabolismus MeSH
- benzoáty chemie metabolismus MeSH
- biodegradace MeSH
- kinetika MeSH
- oxygenasy chemie genetika metabolismus MeSH
- Rhodococcus chemie enzymologie genetika metabolismus MeSH
- substrátová specifita MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- bakteriální proteiny MeSH
- benzoate 1,2-dioxygenase MeSH Prohlížeč
- benzoáty MeSH
- oxygenasy 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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