ω-Transaminase from Ochrobactrum anthropi is devoid of substrate and product inhibitions.
about
Improvement of whole-cell transamination with Saccharomyces cerevisiae using metabolic engineering and cell pre-adaptation.Bacillus anthracis ω-amino acid:pyruvate transaminase employs a different mechanism for dual substrate recognition than other amine transaminases.Exploiting cell metabolism for biocatalytic whole-cell transamination by recombinant Saccharomyces cerevisiae.
P2860
ω-Transaminase from Ochrobactrum anthropi is devoid of substrate and product inhibitions.
description
2013 nî lūn-bûn
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2013年の論文
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2013年論文
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2013年論文
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2013年論文
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2013年论文
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2013年论文
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name
ω-Transaminase from Ochrobactrum anthropi is devoid of substrate and product inhibitions.
@en
type
label
ω-Transaminase from Ochrobactrum anthropi is devoid of substrate and product inhibitions.
@en
prefLabel
ω-Transaminase from Ochrobactrum anthropi is devoid of substrate and product inhibitions.
@en
P2860
P356
P1476
ω-Transaminase from Ochrobactrum anthropi is devoid of substrate and product inhibitions.
@en
P2093
Eul-Soo Park
Jong-Shik Shin
P2860
P304
P356
10.1128/AEM.03811-12
P407
P577
2013-04-12T00:00:00Z