Oxidation of threonine

Vanadate-induced photo-oxidation of serine and subsequent cleavage of the protein were also observed for ribulose-l,5-diphoshate carboxylase/oxygenase from spinach leaves. Activity could be restored by treatment with sodium boronate, which reduces formylglycine back to serine.Similarly, vanadate-induced UV oxidation of threonine (Thr353, at the phosphorylation site) in the sarcoplasmatic reticulum (SR) Ca +-ATPase can be restored by reduction with Na[BH4]. For monovanadate to become catalyti-cally active it is essential that Mg + and ADP bind to the phosphorylation site of the enzyme in its Ca +-receptive conformation, suggesting the formation of an active MgADPV as proposed for the myosin fragmentation. In contrast, decavanadate catalyses the photo-oxidation of a serine (Seri 86) residue in the SR ATPase in the absence of ADP.P bl... 

The oxidation of threonine, valine, methionine, and isoleucine results in propionyl-CoA, which propionyl-CoA carboxylase converts into L-methylmalonyl-CoA, which is metabolized through methylmalonyl-CoA mutase to succinyl-CoA. Whereas the breakdown of the above amino acids is felt to contribute to -50 % of the propiony 1-CoA production, gut bacteria and the breakdown of odd-chain-length fatty acids also substantially contribute to propionyl-CoA production (-25 % each), with a minimal contribution by cholesterol metabolism [10-13] (Fig. 17.1). 

---