MauE and MauD proteins are essential in methylamine metabolism of Paracoccus denitrificans

C.J.N.M. van der Palen, W N Reijnders, S de Vries, J A Duine, R J van Spanning

Research output: Contribution to JournalArticleAcademicpeer-review


Synthesis of enzymes involved in methylamine oxidation via methylamine dehydrogenase (MADH) is encoded by genes present in the mau cluster. Here we describe the sequence of the mauE and mauD genes from Paracoccus denitrificans as well as some properties of mauE and mauD mutants of this organism. The amino acid sequences derived from the mauE and mauD genes showed high similarity with their counterparts in related methylotrophs. Secondary structure analyses of the amino acid sequences predicted that MauE is a membrane protein with five transmembrane-spanning helices and that MauD is a soluble protein with an N-terminal hydrophobic tail. Sequence comparison of MauD proteins from different organisms showed that these proteins have a conserved motif, Cys-Pro-Xaa-Cys, which is similar to a conserved motif found in periplasmic proteins that are involved in the biosynthesis of bacterial periplasmic enzymes containing haem c and/or disulphide bonds. The mauE and mauD mutant strains were unable to grow on methylamine but they grew well on other C1-compounds. These mutants grown under MADH-inducing conditions contained normal levels of the natural electron acceptor amicyanin, but undetectable levels of the beta-subunit and low levels of the alpha-subunit of MADH. It is proposed, therefore, that MauE and MauD are specifically involved in the processing, transport, and/or maturation of the beta-subunit and that the absence of each of these proteins leads to production of a non-functional beta-subunit which becomes rapidly degraded.

Original languageEnglish
Pages (from-to)219-28
Number of pages10
JournalAntonie van Leeuwenhoek
Issue number3
Publication statusPublished - Oct 1997


  • Amino Acid Sequence
  • Bacterial Proteins
  • Cloning, Molecular
  • DNA, Bacterial
  • Methylamines
  • Molecular Sequence Data
  • Oxidoreductases Acting on CH-NH Group Donors
  • Paracoccus denitrificans
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Species Specificity
  • Comparative Study
  • Journal Article
  • Research Support, Non-U.S. Gov't


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