On the structure and linkage of the covalent cofactor of methylamine dehydrogenase from the methylotrophic bacterium W3A1.
Short amino acid sequences around the two linkage sites of the cofactor of methylamine dehydrogenase are presented. Mass spectral data indicates that the covalently bound cofactor is the tricyclic pyrroloquinoline quinone (PQQ). However, the 3 carboxyl groups characteristic of this o-quinone are absent. A cysteine thioether, via a methylene bridge, and a serine ether link the cofactor to the small subunit of methylamine dehydrogenase.
D000595:Amino Acid Sequence; D019605:Euryarchaeota / Q000201:enzymology*; D013058:Mass Spectrometry; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000378:metabolism*; D045542:PQQ Cofactor; D011804:Quinolines / Q000378:metabolism*
D011804:Quinolines; D045542:PQQ Cofactor; C021567:methylamine dehydrogenase; D000587:Oxidoreductases Acting on CH-NH Group Donors