Hyperactive mutants of mouse D-aspartate oxidase: mutagenesis of the active site residue serine 308.

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Role of the active site residues arginine-216 and arginine-237 in the substrate specificity of mammalian D-aspartate oxidase.Effects of dietary leucine supplementation on the gene expression of mammalian target of rapamycin signaling pathway and intestinal development of broilers.

P2860

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Hyperactive mutants of mouse D-aspartate oxidase: mutagenesis of the active site residue serine 308.

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http://www.wikidata.org/entity/Q46781656

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2008 nî lūn-bûn

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2008年の論文

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年学术文章

@zh-hans

2008年学术文章

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2008年学术文章

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2008年學術文章

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2008年學術文章

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Hyperactive mutants of mouse D ...... ctive site residue serine 308.

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Hyperactive mutants of mouse D ...... ctive site residue serine 308.

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type

Item

label

Hyperactive mutants of mouse D ...... ctive site residue serine 308.

@en

Hyperactive mutants of mouse D ...... ctive site residue serine 308.

@nl

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Hyperactive mutants of mouse D ...... ctive site residue serine 308.

@en

Hyperactive mutants of mouse D ...... ctive site residue serine 308.

@nl

P1476

Hyperactive mutants of mouse D ...... ctive site residue serine 308.

@en

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H Homma

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M Katane

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M Sekine

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T Furuchi

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P2860

Three-dimensional structure of the purple intermediate of porcine kidney D-amino acid oxidase. Optimization of the oxidative half-reaction through alignment of the product with reduced flavin

Three-dimensional structure of porcine kidney D-amino acid oxidase at 3.0 A resolution

Effects of hydrogen bonds in association with flavin and substrate in flavoenzyme d-amino acid oxidase. The catalytic and structural roles of Gly313 and Thr317.

On the mechanism of Rhodotorula gracilis D-amino acid oxidase: role of the active site serine 335.

Functional and structural characterization of D-aspartate oxidase from porcine kidney: non-Michaelis kinetics due to substrate activation.

Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the "active-site lid".

Properties of the flavoenzyme d-aspartate oxidase from Octopus vulgaris

P2888

s00726-007-0627-8

P304

75-82

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scholarly article

P356

10.1007/S00726-007-0627-8

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P478

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Toshihiko Hanai

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2008-01-31T00:00:00Z

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P698

18235994

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Hyperactive mutants of mouse D-aspartate oxidase: mutagenesis of the active site residue serine 308.

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P2860

P2860

Hyperactive mutants of mouse D-aspartate oxidase: mutagenesis of the active site residue serine 308.

description

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type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P50

P577

P698

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P50

P577

P698