Title : Arginine-42 and threonine-45 are required for FAD incorporation and catalytic activity in human monoamine oxidase B.

Pub. Date : 1998 Sep 1

PMID : 9724550






7 Functional Relationships(s)
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1 Arginine-42 and threonine-45 are required for FAD incorporation and catalytic activity in human monoamine oxidase B. Flavin-Adenine Dinucleotide monoamine oxidase B Homo sapiens
2 The oxidation of these amine substrates requires the cofactor FAD, which is covalently bound to Cys-397 of human MAO B. Flavin-Adenine Dinucleotide monoamine oxidase B Homo sapiens
3 Previously, Glu-34 and Tyr-44 of MAO B have been identified as residues which engage in noncovalent interactions with FAD that are required for subsequent covalent FAD binding and generation of catalytic activity. Flavin-Adenine Dinucleotide monoamine oxidase B Homo sapiens
4 Previously, Glu-34 and Tyr-44 of MAO B have been identified as residues which engage in noncovalent interactions with FAD that are required for subsequent covalent FAD binding and generation of catalytic activity. Flavin-Adenine Dinucleotide monoamine oxidase B Homo sapiens
5 However, conservative substitutions of Arg-42 with lysine or Thr-45 with serine resulted in MAO B variants that retain both partial activity and partial FAD incorporation. Flavin-Adenine Dinucleotide monoamine oxidase B Homo sapiens
6 These results indicate that Arg-42 and Thr-45 form critical noncovalent interactions with FAD that are required for the subsequent activation of MAO B by covalent coupling of FAD. Flavin-Adenine Dinucleotide monoamine oxidase B Homo sapiens
7 These results indicate that Arg-42 and Thr-45 form critical noncovalent interactions with FAD that are required for the subsequent activation of MAO B by covalent coupling of FAD. Flavin-Adenine Dinucleotide monoamine oxidase B Homo sapiens