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

Fujiwara, K.; Okamura-Ikeda, K.; Motokawa, Y.

Febs Letters 293(1-2): 115-118

1991


ISSN/ISBN: 0014-5793
PMID: 1959641
DOI: 10.1016/0014-5793(91)81164-4
Accession: 040582722

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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.