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1.11.1.18: bromide peroxidase

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

Word Map on EC 1.11.1.18

Reaction

RH
+
HBr
+
H2O2
=
RBr
+ 2 H2O

Synonyms

apobromoperoxidase I, BPO, BPO 1, BPO 2, BPO I, BPO-A1, BPO-A2, BPO1, bpoA1, bromooperoxidase, bromoperoxidase, bromoperoxidase A2, bromoperoxidase I, bromoperoxidase II, bromoperoxidase-catalase, BrPO, CoVBPO, CVBPO, EC 1.11.1.10, haeme-thiolate peroxidase, HAP phytase, metal-free bromoperoxidase, More, non-haem bromoperoxidase, non-haem bromoperoxidase BPO 1, non-haem bromoperoxidase BPO 2, non-haem bromoperoxidase BPO-A2, non-heme haloperoxidases, non-heme-type bromoperoxidase, nonhaem-type bromoperoxidase BPO 1a, nonhaem-type bromoperoxidase BPO 1b, nonhaem-type bromoperoxidase BPO 3, nonheme bromoperoxidase, nVBPO, perhydrolase, rVBPO, St-Phy, sVBPO, V-BPO, V-BrPO, V-containing-haloperoxidase, vanadate haloperoxidase, vanadate-dependent bromoperoxidase I, vanadium bromoperoxidase, vanadium containing bromoperoxidase, vanadium-bromoperoxidase, vanadium-containing bromoperoxidase, vanadium-dependent bromoperoxidase, vanadium-dependent bromoperoxidase 2, vanadium-dependent haloperoxidase, vanadium-dependent peroxidase, vBPO, VBPO1, VBPO2, VBrPO, VBrPO(AnI), VBrPO(AnII)

ECTree

     1 Oxidoreductases
         1.11 Acting on a peroxide as acceptor
             1.11.1 Peroxidases
                1.11.1.18 bromide peroxidase

Subunits

Subunits on EC 1.11.1.18 - bromide peroxidase

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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
dodecamer
-
12 * 64000, SDS-PAGE
homohexamer
bromoperoxidase II comprises six identical subunits. Converging chains of N-terminal peptides are interwoven at dimer-dimer interfaces in a catenane-type manner. Guanidinium stacks between arginine side chains tighten interfaces by hydrogen bond-clamping between prolyl carboxamide and guanidinium groups, being supplemented by attractive forces from arrays of hydrogen-bonded water molecules, for overcoming like/like repulsion. 40% of the bromoperoxidase II solid state secondary structure derive from helices, 10% from beta-strands, 4% from turns, and 46% from coils. Primary and secondary enzyme structure analysis, comparison of the enzyme structure with other enzyme structures, modeled surface polarization of a VBrPO(AnII)-monomer, detailed overview. Every chain, labeled alphabetically from A to F, contains one molecule of orthovanadate. Disulfide bridges connect thiol groups from cysteine(Cys)41 and Cys77 of one chain to Cys77 and Cys41 to the proximal, linking chain A to chain F, B to C, and D to E. Intramolecular disulfide bridges are formed from Cys117 to Cys126, from Cys474 to Cys502, and from Cys603 to Cys613
trimer