The family of sarcosine oxidases: Same reaction, different products

Majd Lahham, Shalinee Jha, Dominic Goj, Peter Macheroux, Silvia Wallner*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review


The subfamily of sarcosine oxidase is a set of enzymes within the larger family of amine oxidases. It is ubiquitously distributed among different kingdoms of life. The member enzymes catalyze the oxidization of an N-methyl amine bond of amino acids to yield unstable imine species that undergo subsequent spontaneous non-enzymatic reactions, forming an array of different products. These products range from demethylated simple species to complex alkaloids. The enzymes belonging to the sarcosine oxidase family, namely, monomeric and heterotetrameric sarcosine oxidase, l-pipecolate oxidase, N-methyltryptophan oxidase, NikD, l-proline dehydrogenase, FsqB, fructosamine oxidase and saccharopine oxidase have unique features differentiating them from other amine oxidases. This review highlights the key attributes of the sarcosine oxidase family enzymes, in terms of their substrate binding motif, type of oxidation reaction mediated and FAD regeneration, to define the boundaries of this group and demarcate these enzymes from other amine oxidase families.

Original languageEnglish
Article number108868
Number of pages19
JournalArchives of Biochemistry and Biophysics
Early online date2 Apr 2021
Publication statusPublished - 15 Jun 2021


  • Alkaloids
  • Coenzyme reoxidation
  • Covalent flavinylation
  • D-amino acid oxidase family
  • Demethylated products
  • FAD
  • Flavoenzymes
  • Sarcosine oxidase family
  • SOX motif

ASJC Scopus subject areas

  • Molecular Biology
  • Biophysics
  • Biochemistry

Fields of Expertise

  • Human- & Biotechnology


  • NAWI Graz

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