Ornithine cyclodeaminase: structure, mechanism of action, and implications for the mu-crystallin family.

@article{Goodman2004OrnithineCS,
  title={Ornithine cyclodeaminase: structure, mechanism of action, and implications for the mu-crystallin family.},
  author={Jessica L. Goodman and Susan C Wang and Shabnam Alam and Frank J Ruzicka and Perry Allen Frey and Joseph E Wedekind},
  journal={Biochemistry},
  year={2004},
  volume={43 44},
  pages={13883-91}
}
Ornithine cyclodeaminase catalyzes the conversion of L-ornithine to L-proline by an NAD(+)-dependent hydride transfer reaction that culminates in ammonia elimination. Phylogenetic comparisons of amino acid sequences revealed that the enzyme belongs to the mu-crystallin protein family whose three-dimensional fold has not been reported. Here we describe the crystal structure of ornithine cyclodeaminase in complex with NADH, refined to 1.80 A resolution. The enzyme consists of a homodimeric fold… CONTINUE READING