Use of indirect site-directed mutagenesis to alter the substrate specificity of methylamine dehydrogenase.

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Mechanisms for control of biological electron transfer reactions Inter-subunit cross-linking of methylamine dehydrogenase by cyclopropylamine requires residue alphaPhe55.Active site aspartate residues are critical for tryptophan tryptophylquinone biogenesis in methylamine dehydrogenase.

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Use of indirect site-directed mutagenesis to alter the substrate specificity of methylamine dehydrogenase.

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http://www.wikidata.org/entity/Q43815811

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2001 nî lūn-bûn

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2001年の論文

@ja

2001年学术文章

@wuu

2001年学术文章

@zh

2001年学术文章

@zh-cn

2001年学术文章

@zh-hans

2001年学术文章

@zh-my

2001年学术文章

@zh-sg

2001年學術文章

@yue

2001年學術文章

@zh-hant

name

Use of indirect site-directed ...... of methylamine dehydrogenase.

@en

Use of indirect site-directed ...... of methylamine dehydrogenase.

@nl

type

Item

label

Use of indirect site-directed ...... of methylamine dehydrogenase.

@en

Use of indirect site-directed ...... of methylamine dehydrogenase.

@nl

prefLabel

Use of indirect site-directed ...... of methylamine dehydrogenase.

@en

Use of indirect site-directed ...... of methylamine dehydrogenase.

@nl

P1476

Use of indirect site-directed ...... of methylamine dehydrogenase.

@en

P2093

Dapeng Sun

http://www.w3.org/2001/XMLSchema#string

Yongting Wang

http://www.w3.org/2001/XMLSchema#string

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Active site structure of methylamine dehydrogenase: hydrazines identify C6 as the reactive site of the tryptophan-derived quinone cofactor

Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity

Refined crystal structure of methylamine dehydrogenase from Paracoccus denitrificans at 1.75 A resolution

Pyrroloquinoline quinone (PQQ) from methanol dehydrogenase and tryptophan tryptophylquinone (TTQ) from methylamine dehydrogenase.

Directed evolution of an aspartate aminotransferase with new substrate specificities

Steady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans.

Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis.

Converting trypsin to chymotrypsin: the role of surface loops.

Redesigning the substrate specificity of an enzyme: isocitrate dehydrogenase.

Deuterium kinetic isotope effect and stopped-flow kinetic studies of the quinoprotein methylamine dehydrogenase.

P304

4119-4122

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/JBC.M109270200

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P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

277

http://www.w3.org/2001/XMLSchema#string

P50

Victor L. Davidson

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2001-12-03T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

11733518

http://www.w3.org/2001/XMLSchema#string

Use of indirect site-directed mutagenesis to alter the substrate specificity of methylamine dehydrogenase.

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P2860

P2860

Use of indirect site-directed mutagenesis to alter the substrate specificity of methylamine dehydrogenase.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698