Cofactory: Sequence-based prediction of cofactor specificity of Rossmann folds.

TitleCofactory: Sequence-based prediction of cofactor specificity of Rossmann folds.
Publication TypeJournal Article
Year of Publication2014
AuthorsGeertz-Hansen HMarcus, Blom N, Feist AM, Brunak S, Petersen TNordahl
PubMed Date2014 Feb 13

Obtaining optimal cofactor balance to drive production is a challenge in metabolically engineered microbial production strains. To facilitate identification of heterologous enzymes with desirable altered cofactor requirements from native content, we have developed Cofactory, a method for prediction of enzyme cofactor specificity using only primary amino acid sequence information. The algorithm identifies potential cofactor binding Rossmann folds and predicts the specificity for the cofactors FAD(H2 ), NAD(H), and NADP(H). The Rossmann fold sequence search is carried out using hidden Markov models whereas artificial neural networks are used for specificity prediction. Training was carried out using experimental data from protein-cofactor structure complexes. The overall performance was benchmarked against an independent evaluation set obtaining Matthews correlation coefficients of 0.94, 0.79, and 0.65 for FAD(H2 ), NAD(H), and NADP(H), respectively. The Cofactory method is made publicly available at Proteins 2014. © 2014 Wiley Periodicals, Inc.

Alternate JournalProteins
PubMed ID24523134
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