Protein Variants | Comment | Organism |
---|---|---|
additional information | chemical synthesis of mono- and dinuclear oxidovanadium(V) complexes of an amine-bis(phenolate) ligand with bromoperoxidase activities, synthetic routes and kinetics of the complexes, NMR studies, kinetics, and mechanism and catalytic cycle, overview. Complex [LV(O)(H2O2)] formed through the oxidation of Br- to Br+ by [LV(O)(O...Br) (H3O)]+ in the presence of H2O2/KBr, can satisfactorily catalyse the oxidative bromination of salicylaldehyde to give 5-bromosalicylaldehyde as a major product along with 3,5-dibromo-salicylaldehyde and 2,3,5-tribromosalicylaldehyde as minor products, in the presence of HClO4 in mixed solvents (H2O : MeOH : THF = 4 : 3 : 2) at 25°C. In the absence of the catalyst, the reaction mixture gives only a 4% conversion of salicylaldehyde to 5-bromosalicylaldehyde. Catalytic parameters for the bromination of salicylaldehyde by KBr/H2O2 (KBr = 40 mmol, H2O2 = 2 ml, i.e. 67 mmol) using two complexes as catalysts | Ascophyllum nodosum |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
additional information | formation of mono- and dinuclear oxidovanadium(V) complexes of an amine-bis(phenolate) ligand with bromoperoxidase activities, synthetic routes and kinetics of the complexes, overview | Ascophyllum nodosum | |
Vanadium | the vanadium ion is ligated to the protein backbone via one histidine nitrogen donor atom, while the oxido moieties are strongly H-bonded to arginine, lysine, histidine and serine amino acids | Ascophyllum nodosum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
RH + HBr + H2O2 | Ascophyllum nodosum | - |
RBr + 2 H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Ascophyllum nodosum | K7ZUA3 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-chloro-5,5-dimethyl-1,3-cyclohexane-dione HBr + H2O2 | 2-chloro-5,5-dimethyl-1,3-cyclohexane-dione (mcd) is the standard substrate for the determination of haloperoxidase activity using H2O2 as the oxidant | Ascophyllum nodosum | ? + 2 H2O | - |
? | |
additional information | the disproportionation reaction of hydrogen peroxide is a bromidemediated reaction, i.e. V-BPO does not catalyze the formation of singlet oxygen in the absence of bromide ions | Ascophyllum nodosum | ? | - |
- |
|
RH + HBr + H2O2 | - |
Ascophyllum nodosum | RBr + 2 H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
BPO | - |
Ascophyllum nodosum |
bromoperoxidase | - |
Ascophyllum nodosum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | - |
assay at | Ascophyllum nodosum |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
vanadate cofactor | - |
Ascophyllum nodosum |
General Information | Comment | Organism |
---|---|---|
evolution | vanadate-dependent haloperoxidases (VHPOs) are the enzymes that catalyze the 2e- oxidation of a halide by H2O2 to the corresponding hypohalous acids, HOX. Thereby, the formed HOX can react with a broad range of organic substrates to form a diverse variety of halogenated compounds. The classification of VHPOs is based on the nature of the halides oxidized, whereby when they catalyse the oxidation of Cl-, Br- or I- in the presence of H2O2, they are designated as chloroperoxidaes (CPOs), while for the oxidation of Br- or I- they are classified as bromoperoxidases (BPOs) and for the oxidation of I- as iodoperoxidases (IPOs) | Ascophyllum nodosum |