NDLI: Biochemical and structural studies of 6-carboxy-5,6,7,8-tetrahydropterin synthase reveal the molecular basis of catalytic promiscuity within the tunnel-fold superfamily.

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Biochemical and structural studies of 6-carboxy-5,6,7,8-tetrahydropterin synthase reveal the molecular basis of catalytic promiscuity within the tunnel-fold superfamily.

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Biochemical and structural studies of 6-carboxy-5,6,7,8-tetrahydropterin synthase reveal the molecular basis of catalytic promiscuity within the tunnel-fold superfamily.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Miles, Zachary D. Mccarty, Reid M. Roberts, Sue A. Bandarian, Vahe
Description	Author Affiliation: Miles ZD ( From the Department of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona 85721.); Roberts SA ( From the Department of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona 85721.); McCarty RM ( From the Department of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona 85721.); Bandarian V ( From the Department of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona 85721 vahe@email.arizona.edu.)
Abstract	6-Pyruvoyltetrahydropterin synthase (PTPS) homologs in both mammals and bacteria catalyze distinct reactions using the same 7,8-dihydroneopterin triphosphate substrate. The mammalian enzyme converts 7,8-dihydroneopterin triphosphate to 6-pyruvoyltetrahydropterin, whereas the bacterial enzyme catalyzes the formation of 6-carboxy-5,6,7,8-tetrahydropterin. To understand the basis for the differential activities we determined the crystal structure of a bacterial PTPS homolog in the presence and absence of various ligands. Comparison to mammalian structures revealed that although the active sites are nearly structurally identical, the bacterial enzyme houses a His/Asp dyad that is absent from the mammalian protein. Steady state and time-resolved kinetic analysis of the reaction catalyzed by the bacterial homolog revealed that these residues are responsible for the catalytic divergence. This study demonstrates how small variations in the active site can lead to the emergence of new functions in existing protein folds.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	34
Volume Number	289
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2014-08-22
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Carbon-Oxygen Lyases Metabolism Escherichia Coli Proteins Chemistry Genetics Catalysis Catalytic Domain Crystallography, X-Ray DNA Primers Models, Molecular Mutagenesis, Site-Directed Protein Conformation Protein Folding Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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