Stereoselectivity and expanded substrate scope of an engineered PLP-dependent aldolase.
about
Engineered L-serine hydroxymethyltransferase from Streptococcus thermophilus for the synthesis of α,α-dialkyl-α-amino acidsMolecular dynamics simulations of the intramolecular proton transfer and carbanion stabilization in the pyridoxal 5'-phosphate dependent enzymes L-dopa decarboxylase and alanine racemase.Rational approaches for engineering novel functionalities in carbon-carbon bond forming enzymes.Controlling reaction specificity in pyridoxal phosphate enzymes.Recent advances in rational approaches for enzyme engineering.
P2860
Stereoselectivity and expanded substrate scope of an engineered PLP-dependent aldolase.
description
2006 nî lūn-bûn
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2006年の論文
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2006年学术文章
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name
Stereoselectivity and expanded substrate scope of an engineered PLP-dependent aldolase.
@en
Stereoselectivity and expanded substrate scope of an engineered PLP-dependent aldolase.
@nl
type
label
Stereoselectivity and expanded substrate scope of an engineered PLP-dependent aldolase.
@en
Stereoselectivity and expanded substrate scope of an engineered PLP-dependent aldolase.
@nl
prefLabel
Stereoselectivity and expanded substrate scope of an engineered PLP-dependent aldolase.
@en
Stereoselectivity and expanded substrate scope of an engineered PLP-dependent aldolase.
@nl
P2093
P356
P1476
Stereoselectivity and expanded substrate scope of an engineered PLP-dependent aldolase.
@en
P2093
Angelo Guainazzi
Celine Amoreira
Donald Hilvert
Florian P Seebeck
Kim K Baldridge
P304
P356
10.1002/ANIE.200602529
P407
P577
2006-10-01T00:00:00Z