Structural analysis of Pseudomonas 1-aminocyclopropane-1-carboxylate deaminase complexes: insight into the mechanism of a unique pyridoxal-5'-phosphate dependent cyclopropane ring-opening reaction.

@article{Karthikeyan2004StructuralAO,
  title={Structural analysis of Pseudomonas 1-aminocyclopropane-1-carboxylate deaminase complexes: insight into the mechanism of a unique pyridoxal-5'-phosphate dependent cyclopropane ring-opening reaction.},
  author={Subramanian Karthikeyan and Qingxian Zhou and Zongbao Zhao and Chai-Lin Kao and Zhihua Tao and Howard Robinson and Hung-Wen Liu and Hong Zhang},
  journal={Biochemistry},
  year={2004},
  volume={43 42},
  pages={13328-39}
}
1-Aminocyclopropane-1-carboxylate (ACC) deaminase is a pyridoxal 5'-phosphate (PLP) dependent enzyme catalyzing the opening of the cyclopropane ring of ACC to give alpha-ketobutyric acid and ammonia as the products. This ring cleavage reaction is unusual because the substrate, ACC, contains no abstractable alpha-proton and the carboxyl group is retained in the product. How the reaction is initiated to generate an alpha-carbanionic intermediate, which is the common entry for most PLP-dependent… CONTINUE READING

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