Narrowing laccase substrate specificity using active site saturation mutagenesis.
about
Directed evolution of CotA laccase for increased substrate specificity using Bacillus subtilis spores.Directed evolution of fungal laccasesUpgrading Laccase Production and Biochemical Properties: Strategies and Challenges.Crystal structure of CotA laccase complexed with 2,2-azinobis-(3-ethylbenzothiazoline-6-sulfonate) at a novel binding site.Pushing the limits of automatic computational protein design: design, expression, and characterization of a large synthetic protein based on a fungal laccase scaffold.Engineering laccases: in search for novel catalysts.Biochemical characterization of a novel laccase from the basidiomycete fungus Cerrena sp. WR1.The kinetic role of carboxylate residues in the proximity of the trinuclear centre in the O2 reactivity of CotA-laccase.
P2860
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P2860
Narrowing laccase substrate specificity using active site saturation mutagenesis.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年学术文章
@wuu
2009年学术文章
@zh
2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
@zh-sg
2009年學術文章
@yue
2009年學術文章
@zh-hant
name
Narrowing laccase substrate specificity using active site saturation mutagenesis.
@en
Narrowing laccase substrate specificity using active site saturation mutagenesis.
@nl
type
label
Narrowing laccase substrate specificity using active site saturation mutagenesis.
@en
Narrowing laccase substrate specificity using active site saturation mutagenesis.
@nl
prefLabel
Narrowing laccase substrate specificity using active site saturation mutagenesis.
@en
Narrowing laccase substrate specificity using active site saturation mutagenesis.
@nl
P1476
Narrowing laccase substrate specificity using active site saturation mutagenesis
@en
P2093
Nirupama Gupta
P304
P356
10.2174/138620709787581675
P577
2009-03-01T00:00:00Z