Studies on the specificity of the tetrapyrrole substrate for human biliverdin-IXalpha reductase and biliverdin-IXbeta reductase. Structure-activity relationships define models for both active sites.

@article{Cunningham2000StudiesOT,
  title={Studies on the specificity of the tetrapyrrole substrate for human biliverdin-IXalpha reductase and biliverdin-IXbeta reductase. Structure-activity relationships define models for both active sites.},
  author={Orla Cunningham and Aisling Dunne and P Sabido and David A. Lightner and Timothy J. Mantle},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 25},
  pages={19009-17}
}
A comparison of the initial rate kinetics for human biliverdin-IXalpha reductase and biliverdin-IXbeta reductase with a series of synthetic biliverdins with propionate side chains "moving" from a bridging position across the central methene bridge (alpha isomers) to a "gamma-configuration" reveals characteristic behavior that allows us to propose distinct models for the two active sites. For human biliverdin-IXalpha reductase, as previously discussed for the rat and ox enzymes, it appears that… CONTINUE READING

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