The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum.

@article{Fujinaga2004TheMS,
  title={The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum.},
  author={Masao Fujinaga and Maia M. Cherney and Hiroshi Oyama and Kohei Oda and Michael N. G. James},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2004},
  volume={101 10},
  pages={
          3364-9
        }
}
The molecular structure of the pepstatin-insensitive carboxyl peptidase from Scytalidium lignicolum, formerly known as scytalidopepsin B, was solved by multiple isomorphous replacement phasing methods and refined to an R factor of 0.230 (R(free) = 0.246) at 2.1-A resolution. In addition to the structure of the unbound peptidase, the structure of a product complex of cleaved angiotensin II bound in the active site of the enzyme was also determined. We propose the name scytalidocarboxyl peptidase… CONTINUE READING

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