Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene

Eur J Biochem. 1999 Mar;260(3):761-7. doi: 10.1046/j.1432-1327.1999.00204.x.


Lipoyltransferase catalyzes the transfer of the lipoyl group from lipoyl-AMP to the lysine residue of the lipoate-dependent enzymes. We isolated human lipoyltransferase cDNA and genomic DNA. The cDNA insert contained a 1119-base pair open reading frame encoding a precursor peptide of 373 amino acids. Predicted amino acid sequence of the protein shares 88 and 31% identity with bovine lipoyltransferase and Escherichia coli lipoate-protein ligase A, respectively. Northern blot analyses of poly(A)+ RNA indicated a major species of about 1.5 kb. mRNA levels of lipoyltransferase were highest in skeletal muscle and heart, showing good correlation with those of dihydrolipoamide acyltransferase subunits of pyruvate, 2-oxoglutarate and branched-chain 2-oxo acid dehydrogenase complexes and H-protein of the glycine cleavage system which accept lipoic acid as a prosthetic group. The human lipoyltransferase gene is a single copy gene composed of four exons and three introns spanning approximately 8 kb of genomic DNA. Some alternatively spliced mRNA species were found by 5'-RACE analysis, and the most abundant species lacks the third exon. The human lipoyltransferase gene was localized to chromosome band 2q11.2 by fluorescence in situ hybridization.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyltransferases / genetics*
  • Amino Acid Sequence
  • Base Sequence
  • Blotting, Northern
  • Chromosome Mapping
  • Chromosomes, Human, Pair 2*
  • Cloning, Molecular
  • DNA, Complementary / analysis
  • Genome, Human
  • Humans
  • Molecular Sequence Data
  • RNA, Messenger / metabolism
  • Tissue Distribution


  • DNA, Complementary
  • RNA, Messenger
  • Acyltransferases

Associated data

  • GENBANK/AB017566
  • GENBANK/AB017567