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Literature summary for 1.11.1.18 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
Search for more literature for 1.11.1.18

Metals/Ions

Metals/Ions Comment Organism Structure
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
RH + Br- + H2O2 + H+ Ascophyllum nodosum
-
 RBr + 2 H2O
-
 ?
RH + I- + H2O2 + H+ Ascophyllum nodosum
-
 RI + 2 H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Ascophyllum nodosum P81701
-
-

Reaction

Reaction Comment Organism Reaction ID
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information vanadium-dependent bromoperoxidases catalyze reactions involving peroxides and bromide or iodide ions Ascophyllum nodosum ?
-
-
RH + Br- + H2O2 + H+
-
 Ascophyllum nodosum RBr + 2 H2O
-
 ?
RH + I- + H2O2 + H+
-
 Ascophyllum nodosum RI + 2 H2O
-
 ?

Synonyms

Synonyms Comment Organism
bromooperoxidase
-
 Ascophyllum nodosum
V-containing-haloperoxidase
-
 Ascophyllum nodosum
vanadium-dependent bromoperoxidase
-
 Ascophyllum nodosum
vanadium-dependent haloperoxidase
-
 Ascophyllum nodosum

Cofactor

Cofactor Comment Organism Structure
vanadate cofactor
-
 Ascophyllum nodosum

General Information

General Information Comment Organism
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
additional information structure of bound peroxidovanadium(V) in the active site of the vanadium-containing haloperoxidases, overview Ascophyllum nodosum
physiological function vanadium-dependent bromoperoxidases catalyze reactions involving peroxides and bromide or iodide ions Ascophyllum nodosum