Site-directed mutagenesis, kinetic and inhibition studies of aspartate ammonia lyase from Bacillus sp. YM55-1.
about
Synthetic and quantum chemical study on the regioselective addition of amines to methyl maleamate.Coenzyme M biosynthesis in bacteria involves phosphate elimination by a functionally distinct member of the aspartase/fumarase superfamily.Single-step purification and characterization of recombinant aspartase of Aeromonas media NFB-5.
P2860
Site-directed mutagenesis, kinetic and inhibition studies of aspartate ammonia lyase from Bacillus sp. YM55-1.
description
2009 nî lūn-bûn
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2009年の論文
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2009年学术文章
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2009年学术文章
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2009年学术文章
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2009年学术文章
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2009年學術文章
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name
Site-directed mutagenesis, kin ...... yase from Bacillus sp. YM55-1.
@en
Site-directed mutagenesis, kin ...... yase from Bacillus sp. YM55-1.
@nl
type
label
Site-directed mutagenesis, kin ...... yase from Bacillus sp. YM55-1.
@en
Site-directed mutagenesis, kin ...... yase from Bacillus sp. YM55-1.
@nl
prefLabel
Site-directed mutagenesis, kin ...... yase from Bacillus sp. YM55-1.
@en
Site-directed mutagenesis, kin ...... yase from Bacillus sp. YM55-1.
@nl
P2093
P1433
P1476
Site-directed mutagenesis, kin ...... yase from Bacillus sp. YM55-1.
@en
P2093
Dick B Janssen
Gerrit J Poelarends
Vinod Puthan Veetil
Wim J Quax
P2860
P304
P356
10.1111/J.1742-4658.2009.07015.X
P407
P577
2009-04-16T00:00:00Z