Purification and some properties of wild-type and N-terminal-truncated ethanolamine ammonia-lyase of Escherichia coli.

No abstract is available for this paper.

• Publication year

  2010

• Venue

  Journal of Biochemistry (Tokyo)

• Publication date

  Unknown publication date

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1093/jb/mvp145PMID 19762342
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Identification of the substrate radical intermediate derived from ethanolamine during catalysis by ethanolamine ammonia-lyase.

  2008cited by this paper
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  2005cited by this paper
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  2005cited by this paper
• The number of functional active sites per molecule of the adenosylcobalamin-dependent enzyme, ethanolamine ammonia-lyase, as determined by a kinetic method.

  2005cited by this paper
• Radical mechanisms in adenosylcobalamin-dependent enzymes.

  2004cited by this paper
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  2004cited by this paper
• Analysis of the electron paramagnetic resonance spectrum of a radical intermediate in the coenzyme B(12)-dependent ethanolamine ammonia-lyase catalyzed reaction of S-2-aminopropanol.

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  1999cited by this paper
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  1999cited by this paper
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  1999cited by this paper
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  1999cited by this paper
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  1999cited by this paper
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