WebMar 20, 2008 · We present here the first quantum mechanical/molecular mechanics (QM/MM) studies of taurine/alpha-ketoglutarate dioxygenase (TauD) enzymes. Our studies are focused on the chemical properties of the oxo-iron species and the effect of the protein environment on its structural and electronic behavior. … WebBackground: TauD is a nonheme iron(II) and α-ketoglutarate (αKG) dependent dioxygenase, and a member of a broader family of enzymes that oxidatively decarboxylate αKG to …
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WebWe now provide in vitro data to support the functional assignment of LipL, the putative TauD enzyme from the A-90289 gene cluster, as a non-heme, Fe(II)-dependent α-KG:UMP dioxygenase that ... WebSep 12, 1997 · Characterization of TauD. The purified enzyme had a specific activity of 1.64 units/mg of protein. Upon storage at −20 °C at a protein concentration of 2.6 mg/ml in … high note 3 student\u0027s book
Taurine/Alpha-Ketoglutarate Dioxygenase – Computational Studies
WebFeb 25, 2015 · The oxidation of cyclohexane by 2 occurs at a rate comparable to that of the oxidation of taurine by the TauD-J enzyme intermediate after adjustment for the different temperatures of measurement. Moreover, compared with other S = 2 complexes characterized to date, the spectroscopic properties of 2 most closely resemble those of … Web-ketoglutarate ( -KG)-dependent enzymes that are generally agreed to follow identical reaction coordinates involving the oxidative decarboxylation of -KG to give an enzyme-bound Fe(IV)-oxo intermediate that is utilized to abstract a hydrogen atom from a prime substrate, taurine for TauD, to yield a car-bon-centered radical (17, 18). WebThe only enzyme of known function showing some similarity with XanA is the E. coliα‐KG‐dependent taurine dioxygenase (TauD) (Eichhorn et al., 1997). While the overall similarity is very low, we found putative Fe(II) binding sites which are similar to those found in the α‐KG‐dependent dioxygenases. high note consulting llc