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  • Title: Lipoylation of H-protein of the glycine cleavage system. The effect of site-directed mutagenesis of amino acid residues around the lipoyllysine residue on the lipoate attachment.
    Author: Fujiwara K, Okamura-Ikeda K, Motokawa Y.
    Journal: FEBS Lett; 1991 Nov 18; 293(1-2):115-8. PubMed ID: 1959641.
    Abstract:
    H-protein of the glycine cleavage system has lipoic acid on the Lys59 residue. Comparison of amino acid sequences around the lipoate attachment site of H-proteins from various sources and acyltransferases of alpha-keto acid dehydrogenase complexes indicated that Gly43, Glu56, Glu63 and Gly70 of bovine H-protein are highly conserved among these proteins. Modification of these conserved residues by site-directed mutagenesis indicated that Glu56 and Gly70 are important for the lipoylation of H-protein and suggested that the proper conformation around the lipoic acid attachment site is required for the association of H-protein to the enzyme responsible for the lipoylation.
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