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Article

The utility of molecular dynamics simulations for understanding site-directed mutagenesis of glycine residues in biotin carboxylase.

Proteins - 1 Mar 2009

Bordelon Tee, Nilsson Lill Sten O, Waldrop Grover L

Abstract excerpt

Biotin carboxylase from Escherichia coli catalyzes the ATP-dependent carboxylation of biotin and is one component of the multienzyme complex acetyl-CoA carboxylase, which catalyzes the committed step in long-chain fatty acid synthesis. Comparison of the crystal structures of biotin carboxylase in the absence and presence of ATP showed a central B-domain closure when ATP was bound. Peptidic NH groups from two...

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PMID: 18704941
DOI: 10.1002/prot.22190

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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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