Local changes in the catalytic site of mammalian histidine decarboxylase can affect its global conformation and stability.

@article{RodrguezCaso2003LocalCI,
  title={Local changes in the catalytic site of mammalian histidine decarboxylase can affect its global conformation and stability.},
  author={Carlos Rodr{\'i}guez-Caso and Daniel Rodr{\'i}guez-Agudo and Aurelio A. Moya-Garc{\'i}a and Ignacio Fajardo and Miguel {\'A}ngel Medina and Vinod Subramaniam and Francisca S{\'a}nchez-Jim{\'e}nez},
  journal={European journal of biochemistry},
  year={2003},
  volume={270 21},
  pages={4376-87}
}
Mature, active mammalian histidine decarboxylase is a dimeric enzyme of carboxy-truncated monomers (approximately 53 kDa). By using a biocomputational approach, we have generated a three-dimensional model of a recombinant 1/512 fragment of the rat enzyme, which shows kinetic constants similar to those of the mature enzyme purified from rodent tissues. This model, together with previous spectroscopic data, allowed us to postulate that the occupation of the catalytic center by the natural… CONTINUE READING

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X-PLOR, Version 3.1. A System for X-Ray Crystallography and NMR

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