In:
FEBS Letters, Wiley, Vol. 293, No. 1-2 ( 1991-11), p. 115-118
Abstract:
H‐protein of the glycine cleavage system has lipoic acid on the Lys 59 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 Gly 43 , Glu 56 , Glu 63 and Gly 70 of bovine H‐protein are highly conserved among these proteins. Modification of these conserved residues by site‐directed mutagenesis indicated that Glu 56 and Gly 70 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.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(91)81164-4
Language:
English
Publisher:
Wiley
Publication Date:
1991
detail.hit.zdb_id:
1460391-3
SSG:
12
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