MG_272_MONOMER_MODIFICATION_001 – protein lysine lipoate ligation

Name
WID MG_272_MONOMER_MODIFICATION_001 View in model
Name protein lysine lipoate ligation View in model
Cross references EC: 2.7.7.63, BioCyc: RXN-8655
 
Classification
Type adduction View in model
 
Reaction
Stoichiometry [c]: LIPOYLAMP + LYS ⇒ AMP + (2) H + LIPOYLLYS View in model
Modification (43) MG_272_MONOMER [c] View in model
 
Catalysis
Enzyme MG_270_MONOMER [c] View in model
 
Energetics
Is spontaneous (pH 7.5, 25C, I = 0) False View in model
 
Kinetics
Forward kinetics Vmax = 48.7 U/mg View in model
 
Associations
Process Process_ProteinModification View in model
 
Comments
Comments Stephens et al observed a homologous lipoate ligation site in E. coli [PUB_0288]. Of the putative ligation sites predicted by Stephens et al we assigned the ligation to the most conserved residue as determined by ClustalW multiple sequence alignment. The kinetic rate of lipoate ligation was measured by Morris et al [PUB_0290].
References

  1. Green DE, Morris TW, Green J, Cronan JE Jr, Guest JR. Purification and properties of the lipoate protein ligase of Escherichia coli. Biochem J 309 ( Pt 3), 853-62 (1995). WholeCell: PUB_0290, PubMed: 7639702

  2. Stephens PE, Darlison MG, Lewis HM, Guest JR. The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the dihydrolipoamide acetyltransferase component. Eur J Biochem 133, 481-9 (1983). WholeCell: PUB_0288, PubMed: 6345153
 
Metadata
Created 2012-10-01 15:08:41
Last updated 2012-10-01 15:16:53