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Inter‐subunit cross‐linking of methylamine dehydrogenase by cyclopropylamine requires residue αPhe55
Author(s) -
Sun Dapeng,
Davidson Victor L
Publication year - 2002
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/s0014-5793(02)02615-7
Subject(s) - chemistry , protein subunit , methylamine , stereochemistry , biochemistry , paracoccus denitrificans , residue (chemistry) , enzyme , gene
Cyclopropylamine is a mechanism‐based inhibitor of the quinoprotein methylamine dehydrogenase (MADH) from Paracoccus denitrificans . The resulting inactivation is accompanied by the formation of a covalent cross‐link between the α and β subunits of MADH. The results of site‐directed mutagenesis studies indicate that Phe55 on the α subunit is required for this process. No cross‐linking is seen with αF55A or αF55I MADH mutants. In contrast, with αF55E MADH cross‐linking of subunits is observed. These results suggest a novel mechanistic role for a phenylalanine residue and the possible importance of protein dynamics in this enzyme mechanism.