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PDBsum entry 2w2b
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References listed in PDB file
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Key reference
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Title
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P-Coumaric acid decarboxylase from lactobacillus plantarum: structural insights into the active site and decarboxylation catalytic mechanism.
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Authors
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H.Rodríguez,
I.Angulo,
B.De las rivas,
N.Campillo,
J.A.Páez,
R.Muñoz,
J.M.Mancheño.
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Ref.
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Proteins, 2010,
78,
1662-1676.
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PubMed id
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Abstract
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p-Coumaric acid decarboxylases (PDCs) catalyze the nonoxidative decarboxylation
of hydroxycinnamic acids to generate the corresponding vinyl derivatives.
Despite the biotechnological relevance of PDCs in food industry, their catalytic
mechanism remains largely unknown. Here, we report insights into the structural
basis of catalysis for the homodimeric PDC from Lactobacillus plantarum (LpPDC).
The global fold of LpPDC is based on a flattened beta-barrel surrounding an
internal cavity. Crystallographic and functional analyses of single-point
mutants of residues located within this cavity have permitted identifying a
potential substrate-binding pocket and also to provide structural evidences for
rearrangements of surface loops so that they can modulate the accessibility to
the active site. Finally, combination of the structural and functional data with
in silico results enables us to propose a two-step catalytic mechanism for
decarboxylation of p-coumaric acid by PDCs where Glu71 is involved in proton
transfer, and Tyr18 and Tyr20 are involved in the proper substrate orientation
and in the release of the CO(2) product.
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