Abstract
Opine dehydrogenases catalyze the reductive condensation of pyruvate with L-amino acids. Biochemical characterization of alanopine dehydrogenase from Arenicola marina revealed that this enzyme is highly specific for L-alanine. Unbiased molecular dynamics simulations with a homology model of alanopine dehydrogenase captured the binding of L-alanine diffusing from solvent to a putative binding region near a distinct helix-kink-helix motif. These results and sequence comparisons reveal how mutations and insertions within this motif dictate the L-amino acid specificity.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alanine / chemistry*
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Alanine / metabolism
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Amino Acid Substitution
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Animals
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Binding Sites
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Diffusion
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Helminth Proteins / chemistry*
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Helminth Proteins / genetics
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Helminth Proteins / metabolism
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Kinetics
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Ligands
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Molecular Dynamics Simulation*
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Oxidoreductases Acting on CH-NH Group Donors / chemistry*
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Oxidoreductases Acting on CH-NH Group Donors / genetics
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Oxidoreductases Acting on CH-NH Group Donors / metabolism
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Polychaeta / chemistry*
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Polychaeta / enzymology
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Protein Binding
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Pyruvic Acid / chemistry*
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Pyruvic Acid / metabolism
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Structural Homology, Protein
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Substrate Specificity
Substances
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Helminth Proteins
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Ligands
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Recombinant Proteins
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Pyruvic Acid
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Oxidoreductases Acting on CH-NH Group Donors
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alanopine dehydrogenase
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Alanine