Residuo di diidrolipoillisina (2-metilpropanoil)transferasi

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residuo di diidrolipoillisina (2-metilpropanoil)transferasi
Modello tridimensionale dell'enzima
Modello tridimensionale dell'enzima
Numero EC2.3.1.168
ClasseTransferasi
Nome sistematico
2-metilpropanoil-CoA:enzima-N6-(diidrolipoil)lisina S-(2-metilpropanoil)transferasi
Altri nomi
diidrolipoil transacilasi; enzima-diidrolipoillisina:2-metilpropanoil-CoA S-(2-metilpropanoil)transferasi; 2-metilpropanoil-CoA:enzima-6-N-(diidrolipoil)lisina S-(2-metilpropanoil)transferasi
Banche datiBRENDA, EXPASY, GTD, PDB (RCSB PDB PDBe PDBj PDBsum)
Fonte: IUBMB
Modifica dati su Wikidata · Manuale

La residuo di diidrolipoillisina (2-metilpropanoil)transferasi è un enzima appartenente alla classe delle transferasi, che catalizza la seguente reazione:

2-metilpropanoil-CoA + enzima N6-(diidrolipoil)lisina ⇄ CoA + enzima N6-(S-[2-metilpropanoil]diidrolipoil)lisina

Un multimero (24-mer) di questo enzima forma il core del complesso multienzimatico della 3-metil-2-ossobutanoato deidrogenasi, e si lega fortemente sia alla 3-metil-2-ossobutanoato deidrogenasi (trasferisce 2-metilpropanoile) (numero EC 1.2.4.4[1]) ed alla diidrolipoil deidrogenasi (numero EC 1.8.1.4[2]). Il gruppo lipoile di questo enzima viene 2-metilpropanoilato in maniera riducente dalla 3-metil-2-ossobutanoato deidrogenasi (trasferisce 2-metilpropanoile), con il 2-metilpropanoile successivamente trasferito al coenzima A (unica direzione osservata della reazione sopra descritta).

In aggiunta al gruppo 2-metilpropanoile, generato quando la 3-metil-2-ossobutanoato deidrogenasi (trasferisce 2-metilpropanoile) agisce sull'ossoacido che corrisponde alla valina, questo enzima trasferisce anche il 3-metilbutanoile ed i gruppi S-2-metilbutanoili, donatigli quando la 3-metil-2-ossobutanoato deidrogenasi (trasferisce 2-metilpropanoile) agisce sugli ossoacidi corrispondenti alla leucina ed alla isoleucina.

Note

  1. ^ (EN) 1.2.4.4, in ExplorEnz — The Enzyme Database, IUBMB.
  2. ^ (EN) 1.8.1.4, in ExplorEnz — The Enzyme Database, IUBMB.

Bibliografia

  • Perham, R.N., Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions, in Annu. Rev. Biochem., vol. 69, 2000, pp. 961–1004, Entrez PubMed 10966480.
  • Wynn, R.M., Davie, J.R., Zhi, W., Cox, R.P. and Chuang, D.T., In vitro reconstitution of the 24-meric E2 inner core of bovine mitochondrial branched-chain α-keto acid dehydrogenase complex: requirement for chaperonins GroEL and GroES, in Biochemistry, vol. 33, 1994, pp. 8962–8968, Entrez PubMed 7913832.
  • Chuang, D.T., Hu, C.C., Ku, L.S., Niu, W.L., Myers, D.E. and Cox, R.P., Catalytic and structural properties of the dihydrolipoyl transacylase component of bovine branched-chain α-keto acid dehydrogenase, in J. Biol. Chem., vol. 259, 1984, pp. 9277–9284, Entrez PubMed 6746648.
  • Massey, L.K., Sokatch, J.R. and Conrad, R.S., Branched-chain amino acid catabolism in bacteria, in Bacteriol. Rev., vol. 40, 1976, pp. 42–54, Entrez PubMed 773366.
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