Methylidene-imidazolone: A novel electrophile for substrate activation

Research output: Contribution to journalArticle

53 Citations (Scopus)

Abstract

The recent three-dimensional structure of histidine ammonia-lyase revealed that the enzyme contains a 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO) ring, which forms autocatalytically from an Ala-Ser143-Gly triad. This novel prosthetic group, which is also present in phenylalanine ammonia-lyase, activates substrates by electrophilic interaction. Modern analytical methods, theoretical calculations and molecular biology tools have given further insight into the mode of action of MIO.

Original languageEnglish
Pages (from-to)512-524
Number of pages13
JournalCurrent Opinion in Chemical Biology
Volume5
Issue number5
DOIs
Publication statusPublished - Oct 1 2001

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Histidine Ammonia-Lyase
Phenylalanine Ammonia-Lyase
Molecular biology
Prosthetics
Molecular Biology
Chemical activation
Substrates
Enzymes
methylidene-imidazolone

ASJC Scopus subject areas

  • Biochemistry

Cite this

Methylidene-imidazolone : A novel electrophile for substrate activation. / Poppe, L.

In: Current Opinion in Chemical Biology, Vol. 5, No. 5, 01.10.2001, p. 512-524.

Research output: Contribution to journalArticle

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