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Literature summary extracted from

  • McLauchlan, C.C.; Murakami, H.A.; Wallace, C.A.; Crans, D.C.
    Coordination environment changes of the vanadium in vanadium-dependent haloperoxidase enzymes (2018), J. Inorg. Biochem., 186, 267-279 .
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.11.1.B2 Vanadium required vanadium as a transition metal ion that readily converts among oxidations states has the potential to support catalytic processes through oxidation/reduction chemistry as well as hydrolytic chemistry. Coordination chemistry of the vanadium(V) center in the different vanadium-haloperoxidases, overview. Once the V-atom reacts with H2O2 and the peroxidovanadium(V) complex forms, a different coordination environment is formed which is critical for facilitation of the catalysis under mild conditions Curvularia inaequalis
1.11.1.B6 Vanadium required vanadium as a transition metal ion that readily converts among oxidations states has the potential to support catalytic processes through oxidation/reduction chemistry as well as hydrolytic chemistry. Coordination chemistry of the vanadium(V) center in the different vanadium-haloperoxidases, overview Zobellia galactanivorans
1.11.1.18 Vanadium required vanadium as a transition metal ion that readily converts among oxidations states has the potential to support catalytic processes through oxidation/reduction chemistry as well as hydrolytic chemistry. Coordination chemistry of the vanadium(V) center in the different vanadium-haloperoxidases, overview Ascophyllum nodosum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.11.1.B2 RH + Br- + H2O2 + H+ Curvularia inaequalis
-
 RBr + 2 H2O
-
 ?
1.11.1.B2 RH + Cl- + H2O2 + H+ Curvularia inaequalis
-
 RCl + 2 H2O
-
 ?
1.11.1.B2 RH + I- + H2O2 + H+ Curvularia inaequalis
-
 RI + 2 H2O
-
 ?
1.11.1.B6 RH + Br- + H2O2 + H+ Zobellia galactanivorans
-
 RBr + 2 H2O
-
 ?
1.11.1.B6 RH + Br- + H2O2 + H+ Zobellia galactanivorans CCUG 47099
-
 RBr + 2 H2O
-
 ?
1.11.1.B6 RH + Br- + H2O2 + H+ Zobellia galactanivorans Dsij
-
 RBr + 2 H2O
-
 ?
1.11.1.B6 RH + Br- + H2O2 + H+ Zobellia galactanivorans DSM 12802
-
 RBr + 2 H2O
-
 ?
1.11.1.B6 RH + Br- + H2O2 + H+ Zobellia galactanivorans CIP 106680
-
 RBr + 2 H2O
-
 ?
1.11.1.B6 RH + Br- + H2O2 + H+ Zobellia galactanivorans NCIMB 13871
-
 RBr + 2 H2O
-
 ?
1.11.1.B6 RH + I- + H2O2 + H+ Zobellia galactanivorans
-
 RI + 2 H2O
-
 ?
1.11.1.B6 RH + I- + H2O2 + H+ Zobellia galactanivorans CCUG 47099
-
 RI + 2 H2O
-
 ?
1.11.1.B6 RH + I- + H2O2 + H+ Zobellia galactanivorans Dsij
-
 RI + 2 H2O
-
 ?
1.11.1.B6 RH + I- + H2O2 + H+ Zobellia galactanivorans DSM 12802
-
 RI + 2 H2O
-
 ?
1.11.1.B6 RH + I- + H2O2 + H+ Zobellia galactanivorans CIP 106680
-
 RI + 2 H2O
-
 ?
1.11.1.B6 RH + I- + H2O2 + H+ Zobellia galactanivorans NCIMB 13871
-
 RI + 2 H2O
-
 ?
1.11.1.18 RH + Br- + H2O2 + H+ Ascophyllum nodosum
-
 RBr + 2 H2O
-
 ?
1.11.1.18 RH + I- + H2O2 + H+ Ascophyllum nodosum
-
 RI + 2 H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.B2 Curvularia inaequalis P49053 Helminthosporium inaequale
-
1.11.1.B6 Zobellia galactanivorans G0LAH5
-
-
1.11.1.B6 Zobellia galactanivorans CCUG 47099 G0LAH5
-
-
1.11.1.B6 Zobellia galactanivorans CIP 106680 G0LAH5
-
-
1.11.1.B6 Zobellia galactanivorans Dsij G0LAH5
-
-
1.11.1.B6 Zobellia galactanivorans DSM 12802 G0LAH5
-
-
1.11.1.B6 Zobellia galactanivorans NCIMB 13871 G0LAH5
-
-
1.11.1.18 Ascophyllum nodosum P81701
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.11.1.B2 RH + Cl- + H2O2 + H+ = RCl + 2 H2O the catalytic cycle imposes changes in the coordination geometry of the vanadium to accommodate the peroxidovanadium(V) intermediate in an environment of as a distorted square pyramidal geometry. During the catalytic cycle, this intermediate converts to a trigonal bipyramidal intermediate before losing the halogen and forming a tetrahedral vanadium-protein intermediate. The catalysis is facilitated by a proton-relay system supplied by the second sphere coordination environment, and the changes in the coordination environment of the vanadium(V) making this process unique among protein catalyzed processes. The active site is very tightly regulated with only minor changes in the coordination geometry. The coordination geometry in the protein structures deviates from that found for both small molecules crystallized in the absence of protein and the reported functional small molecule model compounds. The catalytic mechanism for oxidation of organic substrates catalyzed by haloperoxidases does not change the oxidation state of the vanadium(V) although the vanadium is present as protein bound intermediate with a coordination number altering from four to six Curvularia inaequalis
a
1.11.1.B6 RH + I- + H2O2 + H+ = RI + 2 H2O the catalytic cycle imposes changes in the coordination geometry of the vanadium to accommodate the peroxidovanadium(V) intermediate in an environment of as a distorted square pyramidal geometry. During the catalytic cycle, this intermediate converts to a trigonal bipyramidal intermediate before losing the halogen and forming a tetrahedral vanadium-protein intermediate. The catalysis is facilitated by a proton-relay system supplied by the second sphere coordination environment, and the changes in the coordination environment of the vanadium(V) making this process unique among protein catalyzed processes. The active site is very tightly regulated with only minor changes in the coordination geometry. The coordination geometry in the protein structures deviates from that found for both small molecules crystallized in the absence of protein and the reported functional small molecule model compounds. The catalytic mechanism for oxidation of organic substrates catalyzed by haloperoxidases does not change the oxidation state of the vanadium(V) although the vanadium is present as protein bound intermediate with a coordination number altering from four to six Zobellia galactanivorans
a
1.11.1.18 RH + HBr + H2O2 = RBr + 2 H2O the catalytic cycle imposes changes in the coordination geometry of the vanadium to accommodate the peroxidovanadium(V) intermediate in an environment of as a distorted square pyramidal geometry. During the catalytic cycle, this intermediate converts to a trigonal bipyramidal intermediate before losing the halogen and forming a tetrahedral vanadium-protein intermediate. The catalysis is facilitated by a proton-relay system supplied by the second sphere coordination environment, and the changes in the coordination environment of the vanadium(V) making this process unique among protein catalyzed processes. The active site is very tightly regulated with only minor changes in the coordination geometry. The coordination geometry in the protein structures deviates from that found for both small molecules crystallized in the absence of protein and the reported functional small molecule model compounds. The catalytic mechanism for oxidation of organic substrates catalyzed by haloperoxidases does not change the oxidation state of the vanadium(V) although the vanadium is present as protein bound intermediate with a coordination number altering from four to six Ascophyllum nodosum
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.B2 additional information vanadium-dependent chloroperoxidases catalyze reactions involving peroxides and chloride, bromide, or iodide ions Curvularia inaequalis ?
-
-
1.11.1.B2 RH + Br- + H2O2 + H+
-
 Curvularia inaequalis RBr + 2 H2O
-
 ?
1.11.1.B2 RH + Cl- + H2O2 + H+
-
 Curvularia inaequalis RCl + 2 H2O
-
 ?
1.11.1.B2 RH + I- + H2O2 + H+
-
 Curvularia inaequalis RI + 2 H2O
-
 ?
1.11.1.B6 additional information vanadium-dependent bromoperoxidases catalyze reactions involving peroxides and bromide or iodide ions Zobellia galactanivorans ?
-
-
1.11.1.B6 additional information vanadium-dependent bromoperoxidases catalyze reactions involving peroxides and bromide or iodide ions Zobellia galactanivorans CCUG 47099 ?
-
-
1.11.1.B6 additional information vanadium-dependent bromoperoxidases catalyze reactions involving peroxides and bromide or iodide ions Zobellia galactanivorans Dsij ?
-
-
1.11.1.B6 additional information vanadium-dependent bromoperoxidases catalyze reactions involving peroxides and bromide or iodide ions Zobellia galactanivorans DSM 12802 ?
-
-
1.11.1.B6 additional information vanadium-dependent bromoperoxidases catalyze reactions involving peroxides and bromide or iodide ions Zobellia galactanivorans CIP 106680 ?
-
-
1.11.1.B6 additional information vanadium-dependent bromoperoxidases catalyze reactions involving peroxides and bromide or iodide ions Zobellia galactanivorans NCIMB 13871 ?
-
-
1.11.1.B6 RH + Br- + H2O2 + H+
-
 Zobellia galactanivorans RBr + 2 H2O
-
 ?
1.11.1.B6 RH + Br- + H2O2 + H+
-
 Zobellia galactanivorans CCUG 47099 RBr + 2 H2O
-
 ?
1.11.1.B6 RH + Br- + H2O2 + H+
-
 Zobellia galactanivorans Dsij RBr + 2 H2O
-
 ?
1.11.1.B6 RH + Br- + H2O2 + H+
-
 Zobellia galactanivorans DSM 12802 RBr + 2 H2O
-
 ?
1.11.1.B6 RH + Br- + H2O2 + H+
-
 Zobellia galactanivorans CIP 106680 RBr + 2 H2O
-
 ?
1.11.1.B6 RH + Br- + H2O2 + H+
-
 Zobellia galactanivorans NCIMB 13871 RBr + 2 H2O
-
 ?
1.11.1.B6 RH + I- + H2O2 + H+
-
 Zobellia galactanivorans RI + 2 H2O
-
 ?
1.11.1.B6 RH + I- + H2O2 + H+
-
 Zobellia galactanivorans CCUG 47099 RI + 2 H2O
-
 ?
1.11.1.B6 RH + I- + H2O2 + H+
-
 Zobellia galactanivorans Dsij RI + 2 H2O
-
 ?
1.11.1.B6 RH + I- + H2O2 + H+
-
 Zobellia galactanivorans DSM 12802 RI + 2 H2O
-
 ?
1.11.1.B6 RH + I- + H2O2 + H+
-
 Zobellia galactanivorans CIP 106680 RI + 2 H2O
-
 ?
1.11.1.B6 RH + I- + H2O2 + H+
-
 Zobellia galactanivorans NCIMB 13871 RI + 2 H2O
-
 ?
1.11.1.18 additional information vanadium-dependent bromoperoxidases catalyze reactions involving peroxides and bromide or iodide ions Ascophyllum nodosum ?
-
-
1.11.1.18 RH + Br- + H2O2 + H+
-
 Ascophyllum nodosum RBr + 2 H2O
-
 ?
1.11.1.18 RH + I- + H2O2 + H+
-
 Ascophyllum nodosum RI + 2 H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.11.1.B2 chloroperoxidase
-
 Curvularia inaequalis
1.11.1.B2 V-containing-haloperoxidase
-
 Curvularia inaequalis
1.11.1.B2 vanadium-dependent chloroperoxidase
-
 Curvularia inaequalis
1.11.1.B2 vanadium-dependent haloperoxidase
-
 Curvularia inaequalis
1.11.1.B6 iodooperoxidase
-
 Zobellia galactanivorans
1.11.1.B6 V-containing-haloperoxidase
-
 Zobellia galactanivorans
1.11.1.B6 vanadium-dependent haloperoxidase
-
 Zobellia galactanivorans
1.11.1.B6 vanadium-dependent iodoperoxidase
-
 Zobellia galactanivorans
1.11.1.B6 zobellia_1262
-
 Zobellia galactanivorans
1.11.1.18 bromooperoxidase
-
 Ascophyllum nodosum
1.11.1.18 V-containing-haloperoxidase
-
 Ascophyllum nodosum
1.11.1.18 vanadium-dependent bromoperoxidase
-
 Ascophyllum nodosum
1.11.1.18 vanadium-dependent haloperoxidase
-
 Ascophyllum nodosum

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.B2 vanadate cofactor
-
 Curvularia inaequalis
1.11.1.B6 vanadate cofactor
-
 Zobellia galactanivorans
1.11.1.18 vanadate cofactor
-
 Ascophyllum nodosum

General Information

EC Number General Information Comment Organism
1.11.1.B2 evolution vanadium-dependent haloperoxidases (VPXOs) are a class of enzymes that catalyze selective oxidation reactions for which vanadium is an essential cofactor converting halides to form halogenated organic products and water. These enzymes include chloroperoxidase and bromoperoxidase, which have very different protein sequences and sizes, but regardless the coordination environment of the active sites is constant. Coordination chemistry of the vanadium(V) center in the different vanadium-haloperoxidases, overview Curvularia inaequalis
1.11.1.B2 additional information structure of bound peroxidovanadium(V) in the active site of the vanadium-containing haloperoxidases, overview. The V-atom in the peroxidovanadium(V)-protein complex is in a distorted square pyramidal geometry (SPY-5) but the formation of this intermediate is clearly an important reason supporting the catalysis Curvularia inaequalis
1.11.1.B2 physiological function vanadium-dependent chloroperoxidases catalyze reactions involving peroxides and chloride, bromide, or iodide ions Curvularia inaequalis
1.11.1.B6 evolution vanadium-dependent haloperoxidases (VPXOs) are a class of enzymes that catalyze selective oxidation reactions for which vanadium is an essential cofactor converting halides to form halogenated organic products and water. These enzymes include chloroperoxidase and bromoperoxidase, which have very different protein sequences and sizes, but regardless the coordination environment of the active sites is constant. Coordination chemistry of the vanadium(V) center in the different vanadium-haloperoxidases, overview Zobellia galactanivorans
1.11.1.B6 additional information structure of bound peroxidovanadium(V) in the active site of the vanadium-containing haloperoxidases, overview Zobellia galactanivorans
1.11.1.B6 physiological function vanadium-dependent bromoperoxidases catalyze reactions involving peroxides and bromide or iodide ions Zobellia galactanivorans
1.11.1.18 evolution vanadium-dependent haloperoxidases (VPXOs) are a class of enzymes that catalyze selective oxidation reactions for which vanadium is an essential cofactor converting halides to form halogenated organic products and water. These enzymes include chloroperoxidase and bromoperoxidase, which have very different protein sequences and sizes, but regardless the coordination environment of the active sites is constant. Coordination chemistry of the vanadium(V) center in the different vanadium-haloperoxidases, overview Ascophyllum nodosum
1.11.1.18 additional information structure of bound peroxidovanadium(V) in the active site of the vanadium-containing haloperoxidases, overview Ascophyllum nodosum
1.11.1.18 physiological function vanadium-dependent bromoperoxidases catalyze reactions involving peroxides and bromide or iodide ions Ascophyllum nodosum