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J. Biol. Chem., Vol. 269, Issue 51, 32039-32042, Dec, 1994
D Cai and JP Klinman
Copper amine oxidases are representative of a new class of redox enzymes
that contain a peptide-bound quinone cofactor, generated by
posttranslational modification of amino acid side chain(s). We have
investigated the mechanism for the biogenesis of 2,4,5-
trihydroxyphenylalanine quinone (TPQ) in amine oxidase with two site-
specific mutants of the yeast methylamine oxidase. Our results show that
the capacity for TPQ formation in vivo is abolished when a putative ligand
to copper, His-456, is changed to Asp; this H456D mutant binds copper at a
low level (approximately 4.1%), relative to the wild-type protein. In
contrast, altering the active site consensus sequence that contains the
precursor tyrosine does not affect TPQ production. The data implicate a
self-catalysis mechanism for TPQ biogenesis, in which the protein-bound
copper plays a key role. We propose that the minimal information required
for TPQ biogenesis lies in a structural motif consisting of the copper site
and the precursor tyrosine.
Evidence of a self-catalytic mechanism of 2,4,5-trihydroxyphenylalanine quinone biogenesis in yeast copper amine oxidase
Department of Chemistry, University of California, Berkeley 94720-1460.
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