※ Browse result(s) for Lipoylation

•  There are 25 proteins containing lysine Lipoylation site(s) in the PLMD database

•  About lysine Lipoylation

Lipoylation, the covalent attachment of lipoic acid to 2-oxoacid dehydrogenase multi-enzyme complexes, is essential for metabolism in aerobic bacteria and eukarya. In Escherichia coli, lipoylation is catalysed by LplA (lipoate protein ligase) or by LipA (lipoic acid synthetase) and LipB [lipoyl(octanoyl) transferase] combined. Whereas bacterial and eukaryotic LplAs comprise a single two-domain protein, archaeal LplA function typically involves two proteins, LplA-N and LplA-C.

•  The distribution of species for the modified proteins:

Homo sapiens (4)Mus musculus (0)Saccharomyces cerevisiae (2)Rattus norvegicus (1)
Escherichia coli (3)Emericella nidulans (0)Mycobacterium tuberculosis (0)Arabidopsis thaliana (0)
Oryza sativa (0)Vibrio parahaemolyticus (0)Sulfolobus islandicus (0)Plasmodium falciparum (0)
Bacillus subtilis (2)Spiroplasma eriocheiris (0)Drosophila melanogaster (0)Schistosoma japonicum (0)
Phytophthora sojae (0)Bacillus velezensis (0)Corynebacterium glutamicum (0)Others (13)

•  Please select one organism to view the detailed proteins