Catalytically active inclusion bodies of L-lysine decarboxylase from E. coli for 1,5-diaminopentane production.

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Catalytically active inclusion bodies of L-lysine decarboxylase from E. coli for 1,5-diaminopentane production.

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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Catalytically active inclusion ...... 1,5-diaminopentane production.

@en

Catalytically active inclusion ...... 1,5-diaminopentane production.

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Item

label

Catalytically active inclusion ...... 1,5-diaminopentane production.

@en

Catalytically active inclusion ...... 1,5-diaminopentane production.

@nl

prefLabel

Catalytically active inclusion ...... 1,5-diaminopentane production.

@en

Catalytically active inclusion ...... 1,5-diaminopentane production.

@nl

P1476

Catalytically active inclusion ...... 1,5-diaminopentane production.

@en

P2093

Alexander Grünberger

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Doris Hahn

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Marco Oldiges

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Michael H Limberg

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Ramona Kloss

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Ursula Mackfeld

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P2860

Aggregation as bacterial inclusion bodies does not imply inactivation of enzymes and fluorescent proteins

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Structural insights into the Escherichia coli lysine decarboxylases and molecular determinants of interaction with the AAA+ ATPase RavA

Linkage between the bacterial acid stress and stringent responses: the structure of the inducible lysine decarboxylase

Microbial production of short chain diols

Perspective on opportunities in industrial biotechnology in renewable chemicals

Identification and elimination of the competing N-acetyldiaminopentane pathway for improved production of diaminopentane by Corynebacterium glutamicum

Functional genomics of pH homeostasis in Corynebacterium glutamicum revealed novel links between pH response, oxidative stress, iron homeostasis and methionine synthesis.

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5856

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scholarly article

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10.1038/S41598-018-24070-2

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English

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P478

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Martina Pohl

Ulrich Krauss

Vera D Jäger

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2018-04-11T00:00:00Z

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P698

29643457

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P921

Escherichia coli

P932

5895699

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