The isolation and characterisation of a Saccharomyces cerevisiae gene (LIP2) involved in the attachment of lipoic acid groups to mitochondrial enzymes

FEMS Microbiol Lett. 2001 May 15;199(1):131-6. doi: 10.1111/j.1574-6968.2001.tb10663.x.


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.

MeSH terms

  • Acyltransferases
  • Amino Acid Oxidoreductases / metabolism
  • Amino Acid Sequence
  • Cloning, Molecular
  • Fungal Proteins / chemistry
  • Fungal Proteins / genetics*
  • Fungal Proteins / metabolism*
  • Gene Deletion
  • Genes, Fungal
  • Glycine Dehydrogenase (Decarboxylating)
  • Mitochondria / enzymology
  • Mitochondria / metabolism
  • Molecular Sequence Data
  • Peptide Synthases / genetics
  • Peptide Synthases / metabolism
  • Pyruvate Dehydrogenase Complex / metabolism
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / growth & development
  • Saccharomyces cerevisiae Proteins*
  • Sequence Analysis, DNA
  • Thioctic Acid / metabolism*


  • Fungal Proteins
  • Pyruvate Dehydrogenase Complex
  • Saccharomyces cerevisiae Proteins
  • Thioctic Acid
  • Amino Acid Oxidoreductases
  • GCV2 protein, S cerevisiae
  • Glycine Dehydrogenase (Decarboxylating)
  • Acyltransferases
  • LIP2 protein, S cerevisiae
  • Peptide Synthases
  • lipoate-protein ligase