Protein-derived cofactors are catalytic or redox-active centres in proteins, which are formed by posttranslational modification of one or more amino acid residues.
Keywords: enzyme; catalysis; quinone; amino acid; free radical
Protein‐derived Cofactors
Victor L Davidson, University of Mississippi Medical Center, Jackson, Mississippi, USA
Published online: July 2007
DOI: 10.1002/9780470015902.a0000664.pub2
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Figure 1. Structures of protein-derived cofactors.
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Figure 2. Structures of crosslinked amino acids present at the active site of certain haem-containing enzymes.
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| References | |
| Datta S, Mori Y, Takagi K et al. (2001) Structure of a quinohemoprotein amine dehydrogenase with an uncommon redox cofactor and highly unusual crosslinking. Proceedings of the National Academy of Sciences of the USA 98: 14268–14273. | |
| DuBois JL and Klinman JP (2006) Role of a strictly conserved active site tyrosine in cofactor genesis in the copper amine oxidase from Hansenula polymorpha. Biochemistry 45: 3178–3188. | |
| Firbank SJ, Rogers MS and Wilmot CM (2001) Crystal structure of the precursor of galactose oxidase: An unusual self-processing enzyme. Proceedings of the National Academy of Sciences of the USA 98: 12932–12937. | |
| Ghilada RA, Knudsen GM, Medzihradszky KF et al. (2006) The Met-Tyr-Trp cross-link in Mycobacterium tuberculosis catalase-peroxidase (KatG). Journal of Biological Chemistry 280: 22651–22663. | |
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Structure at 2.7 Å resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody F | |
| Reminton SJ, Wachter RM, Yarbrough DK et al. (2005) zFP538, a yellow-fluorescent protein from Zoanthus, contains a novel three-ring chromophore. Biochemistry 44: 202–212. | |
| Schwede TF, Retey J and Schulz GE (1999) Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile. Biochemistry 38: 5355–5361. | |
| Tolbert WD, Zhang Y, Cottet SE et al. (2003) Mechanism of human S-adenosylmethionine decarboxylase proenzyme processing as revealed by the structure of the S68A mutant. Biochemistry 42: 2386–2395. | |
| Wang SX, Mure M, Medzihradszky KF et al. (1996) A crosslinked cofactor in lysyl oxidase: redox function for amino acid side chains. Science 273: 1078–1083. | |
| Wang Y, Li X, Jones LH et al. (2005) MauG-dependent in vitro biosynthesis of tryptophan tryptophylquinone in methylamine dehydrogenase. Journal of the American Chemical Society 127: 8258–8259. | |
| Further Reading | |
| Brazeau BJ, Johnson BJ and Wilmot CM (2004) Copper-containing amine oxidases. Biogenesis and catalysis; a structural perspective. Archives of Biochemistry and Biophysics 428: 22–31. | |
| Davidson VL (2005) Structure and mechanism of tryptophylquinone enzymes. Bioorganic Chemistry 33: 159–170. | |
| Jeschke G (2005) EPR techniques for studying radical enzymes. Biochimica Biophysica Acta 25: 91–102. | |
| book Klinman JP and Dove JE (eds) (2001) Novel Cofactors. Advances in Protein Chemistry, vol. 58. San Diego, CA: Academic Press. | |
| Okeley NM and van der Donk W (2000) Novel cofactors via posttranslational modifications of enzyme active sites. Chemistry & Biology 7: R159–R171. | |
