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Article

Molecular dynamics and density functional studies of substrate binding and catalysis of arginine deiminase.

The journal of physical chemistry. B - 29 Mar 2007

Wang Canhui, Xu Dingguo, Zhang Lidong, Xie Daiqian, Guo Hua

Abstract excerpt

The active-site dynamics of arginine deiminase (ADI) complexed with the arginine substrate are investigated with ns molecular dynamics for the wildtype ADI and several mutants. It is shown that the substrate is held in the active site by an extensive hydrogen bond network, which may be weakened by substitution of active-site residues. In addition, the initial step of the catalysis is explored in several truncated...

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PMID: 17388453
DOI: 10.1021/jp067541g

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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