Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1937203 | Biochemical and Biophysical Research Communications | 2007 | 6 Pages |
Abstract
The crystal structure of Fe-type nitrile hydratase from Rhodococcus erythropolis AJ270 was determined at 1.3 Å resolution. The two cysteine residues (αCys112 and αCys114) equatorially coordinated to the ferric ion were post-translationally modified to cysteine sulfinic acids. A glutamine residue (αGln90) in the active center gave double conformations. Based on the interactions among the enzyme, substrate and water molecules, a new mechanism of biocatalysis of nitrile hydratase was proposed, in which the water molecule activated by the glutamine residue performed as the nucleophile to attack on the nitrile which was simultaneously interacted by another water molecule coordinated to the ferric ion.
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Authors
Liya Song, Mingzhu Wang, Jiaji Shi, Zhiquan Xue, Mei-Xiang Wang, Shijun Qian,