Grupo prostético

Un grupo prostético es el componente no aminoacídico que forma parte de la estructura de las heteroproteínas o proteínas conjugadas.


No debe confundirse con el cofactor que se une a la apoenzima de las enzimas (ya sea una holoproteína o heteroproteína) por enlace no covalente.

Algunos grupos prostéticos

Grupo prostético Función Distribución
Flavín mononucleótido [1]​ Reacciones redox Bacterias, Archaea y eucariotas
Flavín adenín dinucleótido [1]​ Reacciones redox Bacterias, Archaea y eucariotas
Pirroloquinolina quinona [2]​ Reacciones Redox Bacterias
Fosfato de piridoxal [3]​ Transaminación, descarboxilación y desaminación Bacterias, Archaea y eucariotas
Biotina [4]​ Carboxilación Bacterias, Archaea y eucariotas
Metilcobalamina [5]​ Metilación e isomerización Bacterias, Archaea y eucariotas
Pirofosfato de tiamina [6]​ Descarboxilación Bacterias, Archaea y eucariotas
Hemo [7]​ Reacciones redox Bacterias, Archaea y eucariotas
Molibdopterina [8]​[9]​ Reacciones de oxigenación Bacterias, Archaea y eucariotas
Ácido lipoico [10]​ Reacciones redox Bacterias, Archaea y eucariotas

Referencias

  1. ↑ a b Joosten V, van Berkel WJ (2007). «Flavoenzymes». Curr Opin Chem Biol 11 (2): 195-202. PMID 17275397. 
  2. ↑ Salisbury SA, Forrest HS, Cruse WB, Kennard O (1979). «A novel coenzyme from bacterial primary alcohol dehydrogenases.». Nature 280 (5725): 843-4.  PMID 471057
  3. ↑ Eliot AC, Kirsch JF (2004). «Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations». Annu. Rev. Biochem. 73: 383-415. PMID 15189147. 
  4. ↑ Jitrapakdee S, Wallace JC (2003). «The biotin enzyme family: conserved structural motifs and domain rearrangements». Curr. Protein Pept. Sci. 4 (3): 217-29. PMID 12769720. 
  5. ↑ Banerjee R, Ragsdale SW (2003). «The many faces of vitamin B12: catalysis by cobalamin-dependent enzymes». Annu. Rev. Biochem. 72: 209-47. PMID 14527323. 
  6. ↑ Frank RA, Leeper FJ, Luisi BF (2007). «Structure, mechanism and catalytic duality of thiamine-dependent enzymes». Cell. Mol. Life Sci. 64 (7-8): 892-905. PMID 17429582. 
  7. ↑ Wijayanti N, Katz N, Immenschuh S (2004). «Biology of heme in health and disease». Curr. Med. nicolxitah algarete :l Chem. 11 (8): 981-6. PMID 15078160. 
  8. ↑ Mendel RR, Hänsch R (2002). «Molybdoenzymes and molybdenum cofactor in plants». J. Exp. Bot. 53 (375): 1689-98. PMID 12147719. 
  9. ↑ Mendel RR, Bittner F (2006). «Cell biology of molybdenum». Biochim. Biophys. Acta 1763 (7): 621-35. PMID 16784786. 
  10. ↑ Bustamante J, Lodge JK, Marcocci L, Tritschler HJ, Packer L, Rihn BH (1998). «Alpha-lipoic acid in liver metabolism and disease». Free Radic. Biol. Med. 24 (6): 1023-39. PMID 9607614. 

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