EC Number   |
|---|
    1.11.1.11 | - |
| 1.11.1.11 | construction of a 3-D structural model based on the crystal structure of Pisum sativum Apx, PDB code 1APX |
| 1.11.1.11 | crystals of Cys32Ser-mutant and DTNB-modified enzyme grown using the hanging drop, vapor diffusion method. The 2.0 A X-ray crystal structure of DTNB-modified enzyme shows clear electron density for the TNB group covalently attached to Cys32 in all four molecules of the asymmetric unit, indicating complete and specific modification |
| 1.11.1.11 | homology modeling based on soybean APX, PDBID 1OAF. The substrate binding cavity involves residues at positions 30KSCAPL35, 167RCH169 and 172R wherein ascorbate is accommodated via three H-bonds involving 30Lys at the c-edge of heme. 169His served as a bridge between heme-porphyrin of APX and ascorbate creating a charge relay system. Cd binds at 29EKSCAPL35, a site similar to ascorbate binding site. In a complex with jasmonic acid, 4 H-bonds hold jasmonic acid in a cavity at gamma-edge on the distal side of heme. Cadmium does not replace iron or ascorbate or jasmonic acid but binds electrostatically on the surface at a separate site |
| 1.11.1.11 | homology modeling based on template structure PDB ID 1APX from Pisum sativum |
| 1.11.1.11 | in complex with ascorbate |
| 1.11.1.11 | in complex with salicylhydroxamic acid |
| 1.11.1.11 | modeling of 3-D-structure. The distal histidine is hydrogen-bonded with the side chain of residue Asn71, which in turn is hydrogen-bonded with the backbone carbonyl of a residue Glu65. At the closed proximal site of heme, residue His163 is bound to heme iron and forms a strong hydrogen bond with buried residue Asp208. These six residues constitute the active site and are conserved |
| 1.11.1.11 | modeling of structure based on Leishmania major peroxidase, PDB code 3RIV_A. Residues Glu133, Val127, and Ser301 amino acids may play a key role in the inhibition |
| 1.11.1.11 | modeling of structure. The important active site residues His42, Trp 179, Asp 208 are located near by each other |
