An N-methyl glutamate dehydrogenase from Pseudomonas M.A

Louis B. Hersh, Julian A. Peterson, Aubrey A. Thompson

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

Methylamine-induced cells of Pseudomonas MA (ATCC No. 23819) contain a particulate enzyme system which catalyzes the reaction: 2 N-methyl l-glutamate + O2 → 2 l-glutamate + 2 formaldehyde + (H2O). The stoichiometry of this reaction (2 moles N-methyl l-glutamate utilized per mole of oxygen) suggests that the enzyme is a dehydrogenase. During the oxidation of N-methyl l-glutamate, cytochromes b and c are enzymatically reduced, supporting the conclusion that the enzyme is a respiratory chain-linked dehydrogenase. It is proposed that the function of this enzyme is to activate the methyl group of N-methyl l-glutamate so that it may be further metabolized by this microorganism.

Original languageEnglish
Pages (from-to)115-120
Number of pages6
JournalArchives of Biochemistry and Biophysics
Volume145
Issue number1
DOIs
StatePublished - Jul 1971

Bibliographical note

Funding Information:
1 Support,ed in part by Research 13443 to L. B. H. and Research Grant J. A. P. from the National Institutes and by Research Grant I-391 to L. search Grant to J. A. P. from Welch Foundation. 2 Pollock, unpublished

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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