A LIPOAMIDE DEHYDROGENASE FROM NEISSERIA-MENINGITIDIS HAS A LIPOYL DOMAIN

A protein of molecular weight of 64 kDa (p64k) found in the outer memb rane of Neisseria meningitidis shows a high degree of homology with bo th the lipoyl domain of the acetyltransferase and the entire sequence of the lipoamide dehydrogenase, the E2 and E3 components of the dehydr ogenase multienzyme complexes, respectively. The alignment of the p64k with lipoyl domains and lipoamide dehydrogenases from different speci es is presented. The possible implications of this protein in binding protein-dependent transport are discussed. This is the first lipoamide dehydrogenase reported to have a lipoyl domain. (C) 1995 Wiley-Liss, Inc.