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
Authors:
- Yutaro MotokawaYMYutaro Motokawa
- 1 November 1991
- journal article
- Published by Wiley in FEBS Letters
- Vol. 293 (1-2) , 115-118
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 α‐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.Keywords
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