Trypsin cleavage of human cystathionine beta-synthase into an evolutionarily conserved active core: structural and functional consequences.

@article{Kery1998TrypsinCO,
  title={Trypsin cleavage of human cystathionine beta-synthase into an evolutionarily conserved active core: structural and functional consequences.},
  author={Vladim{\'i}r Kery and L S Poneleit and Jan P Kraus},
  journal={Archives of biochemistry and biophysics},
  year={1998},
  volume={355 2},
  pages={222-32}
}
Cystathionine beta-synthase (CBS) catalyzes the condensation of homocysteine and serine to cystathionine-an irreversible step in the eukaryotic transsulfuration pathway. The native enzyme is a homotetramer or multimer of 63-kDa (551 amino acids) subunits and is activated by S-adenosyl-l-methionine (AdoMet) or by partial cleavage with trypsin. Amino-terminal analysis of the early products of trypsinolysis demonstrated that the first cleavages occur at Lys 30, 36, and 39. The enzyme still retains… CONTINUE READING

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