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Biochemistry (Mosc) 1998 Jun;63(6):629-33

Evidence for indole-3-acetic acid binding site in plant peroxidases. Structural similarity between peroxidases and auxin-binding proteins.

Savitsky PA, Rojkova AM, Tishkov VI, Ouporov IV, Rudenskaya GN, Gazaryan IG

Department of Chemical Enzymology, School of Chemistry, Lomonosov Moscow State University, Moscow, 119899, Russia.

Application of computer methods allowed us to demonstrate that plant peroxidases and auxin-binding proteins contain structurally similar fragments. The mapping of the fragments was done using a model structure of horseradish peroxidase. Five of six structurally similar fragments belong to the distal domain and form a subdomain in plant peroxidases that includes the distal heme-coordinating sequence, LHFHDC (amino acid residues 39-44 in horseradish peroxidase). The existence of a substrate-binding site for indole-3-acetic acid in the distal subdomain comprising helices A (whole), B (middle), C (beginning), and D (whole) and the loop between helices D and D' is discussed.

PMID: 9668202, UI: 98334724