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A new model for the pro‐PQQ cofactor of quinoprotein methylamine dehydrogenase
Author(s) -
Vellieux Frederic M.D.,
Hol Wim G.J.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81145-7
Subject(s) - cofactor , chemistry , pyrroloquinoline quinone , methylamine , stereochemistry , biochemistry , protein subunit , enzyme , gene
A model for the pro‐PQQ cofactor of Thiobacillus versutus methylamine dehydrogenase was fitted into a 2.25 Å resolution electron density distribution for this enzyme. This proposed model of pro‐PQQ consists of a tyrosine‐derived quinone indole bicyclic structure. Linkage of the cofactor to the light subunit of the enzyme occurs via the side chain of glutamate 57, which is itself bound to the side chain of arginine 107 of that subunit. Since the elements of this cofactor are derived from tyrosine, glutamate and arginine, we have named it ‘TGA pro‐PQQ’.