Serine residues cytochrome

After activation, protein kinase C phosphorylates specific serine and threonine residues in target proteins. As with cAMP-stimulated protein kinase, the specific cellular responses to protein kinase C activation depend on the ensemble of target proteins that become phosphorylated in a given cell. Known target proteins include calmodulin, the insulin receptor, / -adrenergic receptor, glucose transporter, HMG-CoA reductase, cytochrome P-450, and tyrosine hydroxylase. 

Ellis, S.W, G.P. Hayhurst, T. Lightfoot, G. Smith, J. Harlow, K. Rowland-Yeo et al. (2000). Evidence that serine 304 is not a key ligand-binding residue in the active site of cytochrome P450 2D6. Biochem. J. 345, 565-571. 

With regard to the genetic determinants of the higher-eukaryotic cytochromes, the available data are circumscribed in view of the experimental difficulties. However, a certain parallelism between the higher and lower forms is becoming apparent. Evidence for a nuclear specification of cytochrome c apoprotein comes from the finding that both the mule and the hinny have an equal mixture of the horse and the donkey types of this protein [38]. At position 47, the cytochrome c of the horse contains a threonyl residue, and that of the donkey, a serine. The mule-and-hinny case represents an instance of non-sex-linked Mendelian inheritance without dominance [38]. 

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