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Title: A global characterization and identification of multifunctional enzymes
Authors: Cheng, X.-Y.
Huang, W.-J.
Hu, S.-C.
Zhang, H.-L.
Wang, H.
Zhang, J.-X.
Lin, H.-H.
Chen, Y.-Z. 
Zou, Q.
Ji, Z.-L.
Issue Date: 18-Jun-2012
Citation: Cheng, X.-Y., Huang, W.-J., Hu, S.-C., Zhang, H.-L., Wang, H., Zhang, J.-X., Lin, H.-H., Chen, Y.-Z., Zou, Q., Ji, Z.-L. (2012-06-18). A global characterization and identification of multifunctional enzymes. PLoS ONE 7 (6) : -. ScholarBank@NUS Repository.
Abstract: Multi-functional enzymes are enzymes that perform multiple physiological functions. Characterization and identification of multi-functional enzymes are critical for communication and cooperation between different functions and pathways within a complex cellular system or between cells. In present study, we collected literature-reported 6,799 multi-functional enzymes and systematically characterized them in structural, functional, and evolutionary aspects. It was found that four physiochemical properties, that is, charge, polarizability, hydrophobicity, and solvent accessibility, are important for characterization of multi-functional enzymes. Accordingly, a combinational model of support vector machine and random forest model was constructed, based on which 6,956 potential novel multi-functional enzymes were successfully identified from the ENZYME database. Moreover, it was observed that multi-functional enzymes are non-evenly distributed in species, and that Bacteria have relatively more multi-functional enzymes than Archaebacteria and Eukaryota. Comparative analysis indicated that the multi-functional enzymes experienced a fluctuation of gene gain and loss during the evolution from S. cerevisiae to H. sapiens. Further pathway analyses indicated that a majority of multi-functional enzymes were well preserved in catalyzing several essential cellular processes, for example, metabolisms of carbohydrates, nucleotides, and amino acids. What's more, a database of known multi-functional enzymes and a server for novel multi-functional enzyme prediction were also constructed for free access at © 2012 Cheng et al.
Source Title: PLoS ONE
ISSN: 19326203
DOI: 10.1371/journal.pone.0038979
Appears in Collections:Staff Publications

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