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1.11.1.11: L-ascorbate peroxidase

This is an abbreviated version!
For detailed information about L-ascorbate peroxidase, go to the full flat file.

Word Map on EC 1.11.1.11

Reaction

2 L-ascorbate +

H2O2
+ 2 H+ = 2 monodehydroascorbate + 2 H2O

Synonyms

Am-pAPX1, APEX2, APOX, APX, APX 1, APX 2, APX1, APX2, APX3, APX4, APX5, APX6, APX7, APx8, APXS, APXT, ascorbate peroxidase, ascorbate peroxidase 1, ascorbate peroxidase 2, ascorbate peroxidase 3, ascorbate peroxidase 4, ascorbate peroxidase 5, ascorbate peroxidase 6, ascorbate peroxidase 7, ascorbate peroxidase 8, ascorbate peroxidase6, ascorbic acid peroxidase, At1g07890, AT1G77490, AT3G09640, AT4G08390, AT4G32320, AT4G35000, AT4G35970, AtAPx08, AtAPX1, AtAPX2, AtAPX3, AtAPX5, AtAPX6, AtSAPX, AtstAPX, AtTAPX, cAPX, cAPX 2, CmstAPX, CrAPX4, CreAPX1, CreAPX2, CreAPX4, CreAPXheme, CsAPX1, cytoplasmic ascorbate peroxidase 1, cytosolic ascorbate peroxidase, GhAPX1, glyoxysomal APX, HvAPX1, L-ascorbate peroxidase, L-ascorbate peroxidase 3, L-ascorbate peroxidase 5, L-ascorbate peroxidase 6, L-ascorbate peroxidase, heme-containing, L-ascorbic acid peroxidase, L-ascorbic acid-specific peroxidase, LmAPX, MaAPX1, OsAPx1, OsAPx2, OsAPx3, OsAPx4, OsAPx5, OsAPx6, OsAPx7, OsAPx8, OsAPXa, OsAPXb, pAPX, Pavirv00022559m, peroxidase, ascorbate, peroxisomal ascorbate peroxidase, PgAPX1, PHYPA_001206, PHYPA_001884, PHYPA_021776, PHYPA_024580, PHYPA_024582, Potri.002G081900, Potri.004G174500, Potri.005G112200, Potri.005G161900, Potri.005G179200, Potri.006G089000, Potri.006G132200, Potri.006G254500, Potri.009G015400, Potri.009G134100, Potri.016G084800, PpAPX, PpAPX-S, PpAPX2, PpAPX2.1, PpAPX2.2, PpAPX3, PpAPX6-related, PtAPX-S.1, PtAPX-S.2, PtAPX-TL29, PtAPX.3, PtAPX1.1, PtAPX1.2, PtAPX2, PtAPX3, PtAPX5, PtAPX5-like, PtAPX6 related, PtotAPX, RcAPX, sAPX, stromal APX, stromal ascorbate peroxidase, stromal ascorbate peroxidases, TaAPX, tAPX, thylakoid ascorbate peroxidase, thylakoid membrane-bound ascorbate peroxidases, thylakoid-bound ascorbate peroxidase

ECTree

     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.11 L-ascorbate peroxidase

Crystallization

Crystallization on EC 1.11.1.11 - L-ascorbate peroxidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
construction of a 3-D structural model based on the crystal structure of Pisum sativum Apx, PDB code 1APX
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
in complex with ascorbate
in complex with salicylhydroxamic acid
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
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
modeling of structure. The important active site residues His42, Trp 179, Asp 208 are located near by each other
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
-
of the recombinant enzyme, using the hanging drop, vapor diffusion method, the recombinant enzyme forms monoclinic crystals in space group C2 with a: 132.80 A, b: 53.26 A, c: 171.96 A and beta: 106.93°
-
the crystal structures of the CCP2APX and CCP2APX/F191 mutants are solved
-
homology modeling based on template structure PDB ID 1APX from Pisum sativum