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Review
. 2010 Jan 1;493(1):13-25.
doi: 10.1016/j.abb.2009.07.019. Epub 2009 Aug 3.

Oxidation of amines by flavoproteins

Affiliations
Review

Oxidation of amines by flavoproteins

Paul F Fitzpatrick. Arch Biochem Biophys. .

Abstract

Many flavoproteins catalyze the oxidation of primary and secondary amines, with the transfer of a hydride equivalent from a carbon-nitrogen bond to the flavin cofactor. Most of these amine oxidases can be classified into two structural families, the D-amino acid oxidase/sarcosine oxidase family and the monoamine oxidase family. This review discusses the present understanding of the mechanisms of amine and amino acid oxidation by flavoproteins, focusing on these two structural families.

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Figures

Figure 1
Figure 1
Structures of representative member of monoamine oxidase family of flavin amine oxidases. The figures were constructed using the pdb files 1yy5, 1f8s, 2h94, and 1gos.
Figure 2
Figure 2
Structures of representative member of D-amino acid oxidase family of flavin amine oxidases. The figures were constructed using the pdb files 1eli, 1kif, 1pj6, and 1ng4.
Figure 3
Figure 3
Overlay of the active sites of pig kidney D-amino acid oxidase (red residues) with benzoate (green) and monomeric sarcosine oxidase (purple residues) with pyrrole-2-carboxylate (gold). The flavins in the two proteins were superimposed to create the alignment.
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References

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    1. Müller F. In: Chemistry and Biochemistry of Flavoenzymes. Muller F, editor. I. CRC Press; Boca Raton: 1991. pp. 1–71.
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