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PDBsum entry 2q0s
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References listed in PDB file
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Key reference
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Title
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Structure of a novel enzyme that catalyzes acyl transfer to alcohols in aqueous conditions.
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Authors
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I.Mathews,
M.Soltis,
M.Saldajeno,
G.Ganshaw,
R.Sala,
W.Weyler,
M.A.Cervin,
G.Whited,
R.Bott.
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Ref.
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Biochemistry, 2007,
46,
8969-8979.
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PubMed id
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Abstract
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The unusual architecture of the enzyme (MsAcT) isolated from Mycobacterium
smegmatis forms the mechanistic basis for favoring alcoholysis over hydrolysis
in water. Unlike hydrolases that perform alcoholysis only under anhydrous
conditions, MsAcT demonstrates alcoholysis in substantially aqueous media and,
in the presence of hydrogen peroxide, has a perhydrolysis:hydrolysis ratio
50-fold greater than that of the best lipase tested. The crystal structures of
the apoenzyme and an inhibitor-bound form have been determined to 1.5 A
resolution. MsAcT is an octamer in the asymmetric unit and forms a tightly
associated aggregate in solution. Relative to other structurally similar
monomers, MsAcT contains several insertions that contribute to the
oligomerization and greatly restrict the shape of the active site, thereby
limiting its accessibility. These properties create an environment by which
MsAcT can catalyze transesterification reactions in an aqueous medium and
suggests how a serine hydrolase can be engineered to be an efficient
acyltransferase.
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