Crystal structure of Haemophilus influenzae 3-isopropylmalate dehydrogenase (LeuB) in complex with the inhibitor O -isobutenyl oxalylhydroxamate
作者: Riccardo MiggianoSara MartignonAlberto MinassiFranca RossiMenico Rizzi
作者单位: 1Department of Pharmaceutical Sciences, University of Piemonte Orientale, Via Bovio 6, 28100, Novara, Italy
刊名: Biochemical and Biophysical Research Communications, 2020, Vol.524 (4), pp.996-1002
来源数据库: Elsevier Journal
DOI: 10.1016/j.bbrc.2020.02.022
关键词: Haemophilus influenzaeLeucine biosynthesis3-Isopropylmalate dehydrogenaseInhibitorCrystal structure
原始语种摘要: Abstract(#br)3-isopropylmalate dehydrogenases (LeuB) belong to the leucine biosynthetic pathway and catalyze the irreversible oxidative decarboxylation of 3IPM to 2-ketoisocaproate that is finally converted into leucine by a branched-chain aminotransferase. Since leucine is an essential amino acid for humans, and it is also vital for the growth of many pathogenic bacteria, the enzymes belonging to this pathway can be considered as potential target sites for designing of a new class of antibacterial agents. We have determined the crystal structure of the Haemophilus influenzae LeuB in complex with the cofactor NAD + and the inhibitor O -IbOHA, at 2.1 Å resolution; moreover, we have investigated the inhibitor mechanism of action by analyzing the enzyme kinetics. The structure of H....
全文获取路径: Elsevier  (合作)

  • dehydrogenase 脱氢酶
  • complex 超群
  • inhibitor 抑制剂
  • structure 构造