
The isolation and characterisation of a Saccharomyces cerevisiae gene ( LIP2 ) involved in the attachment of lipoic acid groups to mitochondrial enzymes
Author(s) -
Marvin Marcus E.,
Williams Peter H.,
Cashmore Annette M.
Publication year - 2001
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2001.tb10663.x
Subject(s) - lipoic acid , pyruvate dehydrogenase complex , biochemistry , kluyveromyces lactis , saccharomyces cerevisiae , thioctic acid , biology , pyruvate decarboxylase , cofactor , carboxy lyases , dihydrolipoyl transacetylase , enzyme , gene , pyruvate decarboxylation , alcohol dehydrogenase , antioxidant
Lipoic acid is an essential cofactor for a variety of mitochondrial enzymes. We have characterised a gene from Saccharomyces cerevisiae which appears to encode a protein involved in the attachment of lipoic acid groups to the pyruvate dehydrogenase and glycine decarboxylase complexes. The predicted protein product of this gene has significant identity to the lipoyl ligase B of both Escherichia coli and Kluyveromyces lactis . A strain harbouring a null allele of this S. cerevisiae gene is respiratory deficient due to inactive pyruvate dehydrogenase, and is unable to utilise glycine as a sole nitrogen source.