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PDBsum entry 3iae
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References listed in PDB file
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Key reference
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Title
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Active-Site engineering of benzaldehyde lyase shows that a point mutation can confer both new reactivity and susceptibility to mechanism-Based inhibition.
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Authors
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G.S.Brandt,
M.M.Kneen,
G.A.Petsko,
D.Ringe,
M.J.Mcleish.
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Ref.
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J Am Chem Soc, 2010,
132,
438-439.
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PubMed id
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Abstract
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Benzaldehyde lyase (BAL) from Pseudomonas putida is a thiamin diphosphate
(ThDP)-dependent enzyme that catalyzes the breakdown of (R)-benzoin. Here we
report that a point mutant, BAL A28S, not only catalyzes the decarboxylation of
benzoylformate but, like benzoylformate decarboxylase (BFDC), is also
inactivated by the benzoylformate analogues methyl benzoylphosphonate (MBP) and
benzoylphosphonate (BP). The latter has no effect on wild-type BAL, and the
inactivation of the A28S variant is shown to result from phosphorylation of the
newly introduced serine residue. This lends support to the proposal that an
appropriately placed nucleophile facilitates the expulsion of carbon dioxide
from the active site in many ThDP-dependent decarboxylases.
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