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Information on EC 1.11.1.B2 - chloride peroxidase (vanadium-containing)
for references in articles please use BRENDA:EC1.11.1.B2
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preliminary BRENDA-supplied EC number
EC Tree 1 Oxidoreductases
1.11 Acting on a peroxide as acceptor
1.11.1 Peroxidases
1.11.1.B2 chloride peroxidase (vanadium-containing)
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 1.11.1.B2
- inaequalis
-
curvularia
- vanadate
- halide
-
bromoperoxidase
-
chlorination
-
vhpos
-
meroterpenoids
- glucose-6-phosphatase
- nodosum
-
ascophyllum
-
corallina
- prenyltransferase
-
peroxo
-
vanadiumv
-
bipyramidal
- seaweeds
-
td-dft
- diagnostics
- synthesis
Synonyms
vanadium chloroperoxidase, vanadium-dependent haloperoxidase, vanadium haloperoxidase, vanadium-dependent chloroperoxidase, vanadium-containing chloroperoxidase, naph1, mcl24, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CPO
NapH1
vanadium chloroperoxidase
vanadium-dependent chloroperoxidase
vanadium-dependent haloperoxidase
vCPO
VHPO
additional information
vanadium chloroperoxidase
-
vCPO
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
RH + Cl- + H2O2 + H+ = RCl + 2 H2O
Brings about the chlorination of a range of organic molecules, forming stable C-Cl bonds. Can also act on bromide and iodide ions. Instead of the heem group of EC 1.11.1.10, the enzymes of this group contain vanadium (V) bound to the active centre. Since the actual halogenating agents are the respective hypohalous acids (like in the case of EC 1.11.1.10), vanadium-containing halide peroxidases lack substrate specificity and regioselectivity.
-
-
-
RH + Cl- + H2O2 + H+ = RCl + 2 H2O
QM/MM calculations are used to study the structural properties, ground state energies, NMR and UVĀvis spectra of different models of the resting states of the vanadium dependent chloroperoxidase
RH + Cl- + H2O2 + H+ = RCl + 2 H2O
biosynthesis of hypochlorite proceeds in two steps: H2O2 activation on the vanadium center to form an end-on V(V)-hydroperoxo complex, followed by OH+ transfer from hydroperoxo to chloride on the vanadium center to form hypochlorite. The initial reaction starts with a proton transfer from H2O2 to the equatorial OH group of the VV(O)2(OH)2- active site, followed by hydroperoxo binding and water release to form the highly stable vanadium-hydroperoxo-dioxo-hydroxo complex. A further proton transfer from an active-site His or Lys residue can lead to the vanadium-peroxo-hydroxo-oxo complex, which is assign as a dead-end complex unable to react further to hypochlorite products. The mechanisms are considered under various protonation state, and the most effective is the one with His404 singly protonated. Vanadium is a spectator ion that does not change its oxidation state during the reaction mechanism but holds and positions the H2O2 substrate and guides its proton-relay steps through its oxo and hydroxo ligands. The reaction is highly sensitive to local changes in the protonation state. The oxygen atom of HOCl exclusively derives from H2O2
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
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SYSTEMATIC NAME
IUBMB Comments
chloride:hydrogen-peroxide oxidoreductase (vanadium-containing)
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,1-dimethyl-4-chloro-3,5-cyclohexanedione + Cl- + H2O
?
Substrates: -
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?
2 3-chloro-4-(3-chloro-2-nitrophenyl)pyrrole + 3 Cl- + H2O2
2,3-dichloro-4-(3-chloro-2-nitrophenyl)pyrrole + 2,3,5-trichloro-4-(3-chloro-2-nitrophenyl)pyrrole
3-chloro-2-[(2E)-3,7-dimethylocta-2,6-dien-1-yl]-2,5,7-trihydroxy-6-methyl-3-(3-methylbut-2-en-1-yl)-2,3-dihydronaphthalene-1,4-dione + bromide + H2O2
(3R)-3-bromo-4a-chloro-10a-[(2E)-3,7-dimethylocta-2,6-dien-1-yl]-6,8-dihydroxy-2,2,7-trimethyl-3,4,4a,10a-tetrahydro-2H-benzo[g]chromene-5,10-dione + H+
-
Substrates: -
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?
3-chloro-2-[(2E)-3,7-dimethylocta-2,6-dien-1-yl]-2,5,7-trihydroxy-6-methyl-3-(3-methylbut-2-en-1-yl)-2,3-dihydronaphthalene-1,4-dione + chloride + H2O2
(3R)-3,4a-dichloro-10a-[(2E)-3,7-dimethylocta-2,6-dien-1-yl]-6,8-dihydroxy-2,2,7-trimethyl-3,4,4a,10a-tetrahydro-2H-benzo[g]chromene-5,10-dione + H+
-
Substrates: -
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?
Cl- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
Substrates: i.e. monochlorodimedone
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?
cyclohexene + KBr + H2O2
2-bromocyclohexan-1-ol + 2 H2O
Substrates: -
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?
hept-1-ene + KBr + H2O2
1-bromoheptan-2-ol + 2 H2O
Substrates: -
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?
methyl p-tolyl sulfide + H2O2
p-tolyl methyl sulfoxide
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Substrates: in absence of Cl- the oxidation is enantioselective and an oxygen atom of H2O2 is incorporated in the sulfoxide, in the presence of Cl- the oxidation is not enantioselective and there is no incorporation of oxygen from H2O2. The sulfide oxidation takes place through an enzyme-generated freely dissociable oxidized halogen intermediate formed by the interaction of enzyme-OCl- with Cl-
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?
monochlorodimedone + Br- + H2O2
monobromo-monochlorodimedone + H2O
Substrates: -
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?
monochlorodimedone + bromide + H2O2 + H+
bromochlorodimedone + 2 H2O
Substrates: -
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?
monochlorodimedone + chloride + H2O2
dichlorodimedone + H2O
-
Substrates: -
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?
monochlorodimedone + chloride + H2O2 + H+
dichlorodimedone + H2O
Substrates: -
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?
monochlorodimedone + Cl- + H2O2
dichlorodimedone + H2O
Substrates: -
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?
pre-merochlorin + Cl- + H+ + H2O2
merochlorin A + merochlorin B + 2 H2O
Substrates: -
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?
styrene + KBr + H2O2
2-bromo-1-phenylethan-1-ol + 2-phenyloxirane + 2 H2O
Substrates: -
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?
styrene + KCl + H2O2
2-chloro-1-phenylethan-1-ol + 2 H2O
Substrates: -
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?
[(1E)-prop-1-en-1-yl]benzene + KBr + H2O2
(1R,2R)-2-bromo-1-phenylpropan-1-ol + 2 H2O
Substrates: -
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?
[(1Z)-prop-1-en-1-yl]benzene + KBr + H2O2
(1R,2S)-2-bromo-1-phenylpropan-1-ol + 2 H2O
Substrates: -
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?
1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane + Cl- + H2O2
additional information
-
2 3-chloro-4-(3-chloro-2-nitrophenyl)pyrrole + 3 Cl- + H2O2
2,3-dichloro-4-(3-chloro-2-nitrophenyl)pyrrole + 2,3,5-trichloro-4-(3-chloro-2-nitrophenyl)pyrrole
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Substrates: chlorination in the pyrrole ring
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?
2 3-chloro-4-(3-chloro-2-nitrophenyl)pyrrole + 3 Cl- + H2O2
2,3-dichloro-4-(3-chloro-2-nitrophenyl)pyrrole + 2,3,5-trichloro-4-(3-chloro-2-nitrophenyl)pyrrole
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Substrates: chlorination in the pyrrole ring
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?
2 3-chloro-4-(3-chloro-2-nitrophenyl)pyrrole + 3 Cl- + H2O2
2,3-dichloro-4-(3-chloro-2-nitrophenyl)pyrrole + 2,3,5-trichloro-4-(3-chloro-2-nitrophenyl)pyrrole
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Substrates: chlorination in the pyrrole ring
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?
4-(2-amino-3-chlorophenyl)pyrrole + Cl- + H2O2
aminopyrrolnitrin + ?
-
Substrates: -
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?
4-(2-amino-3-chlorophenyl)pyrrole + Cl- + H2O2
aminopyrrolnitrin + ?
-
Substrates: enzyme is involved in the biosynthesis of the antibiotic pyrrolnitrin
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?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
Substrates: i.e. monochlorodimedone
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?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
Substrates: i.e. monochlorodimedone, brominating activity of chloroperoxidase
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?
Cl- + H2O2 + H+
HOCl + H2O
Substrates: -
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?
indole + Cl- + H2O2
oxindole + monochloroindole + H2O
-
Substrates: -
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?
indole + Cl- + H2O2
oxindole + monochloroindole + H2O
-
Substrates: -
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?
indole + Cl- + H2O2
oxindole + monochloroindole + H2O
-
Substrates: -
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?
indole + Cl- + H2O2
oxindole + monochloroindole + H2O
-
Substrates: -
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?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
-
Substrates: no activity
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?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
Substrates: -
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?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
-
Substrates: -
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?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
Substrates: -
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?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
-
Substrates: no activity
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?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
-
Substrates: no activity
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?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
-
Substrates: no activity
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?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
-
Substrates: no activity
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?
monochlorodimedone + Br- + H2O2
?
-
Substrates: -
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?
monochlorodimedone + Br- + H2O2
?
-
Substrates: -
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?
monochlorodimedone + Br- + H2O2
?
-
Substrates: all bacterial nonheme haloperoxidases catalyze the bromination, but not the chlorination of monochlorodimedone. Therefore, they are isolated as bromoperoxidases. While the bromination of organic compounds is very unspecific, a substrate specificity exists for the chlorination. Appropriate substrates such as indole or phenyl pyrrole derivatives are chlorinated
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?
monochlorodimedone + Br- + H2O2
?
-
Substrates: all bacterial nonheme haloperoxidases catalyze the bromination, but not the chlorination of monochlorodimedone. Therefore, they are isolated as bromoperoxidases. While the bromination of organic compounds is very unspecific, a substrate specificity exists for the chlorination. Appropriate substrates such as indole or phenyl pyrrole derivatives are chlorinated
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?
RH + Cl- + H2O2 + H+
RCl + 2 H2O
Substrates: -
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?
1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane + Cl- + H2O2
additional information
-
Substrates: -
Products: uncleaved chlorinated derivatives of 1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane + 1-chloro-4-ethoxy-3-methoxybenzene + 1,2-dichloro-4-ethoxy-5-methoxybenzene. 1-chloro-4-ethoxy-3-methoxybenzene and 1,2-dichloro-4-ethoxy-5-methoxybenzene are cleavage products of the chlorinated derivatives of 1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane
Products: uncleaved chlorinated derivatives of 1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane + 1-chloro-4-ethoxy-3-methoxybenzene + 1,2-dichloro-4-ethoxy-5-methoxybenzene. 1-chloro-4-ethoxy-3-methoxybenzene and 1,2-dichloro-4-ethoxy-5-methoxybenzene are cleavage products of the chlorinated derivatives of 1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane
?
1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane + Cl- + H2O2
additional information
-
-
Substrates: -
Products: uncleaved chlorinated derivatives of 1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane + 1-chloro-4-ethoxy-3-methoxybenzene + 1,2-dichloro-4-ethoxy-5-methoxybenzene. 1-chloro-4-ethoxy-3-methoxybenzene and 1,2-dichloro-4-ethoxy-5-methoxybenzene are cleavage products of the chlorinated derivatives of 1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane
Products: uncleaved chlorinated derivatives of 1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane + 1-chloro-4-ethoxy-3-methoxybenzene + 1,2-dichloro-4-ethoxy-5-methoxybenzene. 1-chloro-4-ethoxy-3-methoxybenzene and 1,2-dichloro-4-ethoxy-5-methoxybenzene are cleavage products of the chlorinated derivatives of 1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane
?
additional information
?
-
-
Substrates: no peroxidase activity, no catalase activity
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?
additional information
?
-
Substrates: oxidation of 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
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?
additional information
?
-
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Substrates: oxidation of 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
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?
additional information
?
-
Substrates: repression by addition of glucose
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?
additional information
?
-
-
Substrates: repression by addition of glucose
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?
additional information
?
-
Substrates: the enzyme may have a role in the natural production of high-molecular-weight chloroaromatics and in lignin breakdown
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?
additional information
?
-
Substrates: the alkalophilic P395D/L241V/T343A mutant of vanadium chloroperoxidase shows bactericidal and virucidal activity
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?
additional information
?
-
Substrates: catalytic cycle and function of the vanadium atom in the reaction mechanism, computational study using large cluster model complexes, possible pathways, and active-site protonation states, overview
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-
additional information
?
-
Substrates: vanadium-dependent chloroperoxidases catalyze reactions involving peroxides and chloride, bromide, or iodide ions
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-
additional information
?
-
-
Substrates: prochiral selectivity in H2O2-promoted oxidation of arylalkanols, the cleavage of the pro-S C-H bond always predominating over the cleavage of the pro-R C-H bond
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?
additional information
?
-
-
Substrates: the enzyme may have a role in the natural production of high-molecular-weight chloroaromatics and in lignin breakdown
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?
additional information
?
-
Substrates: no substrates: geraniol and nerolidol or substrate analogues closely resembling the physiological substrate pre-merochlorin
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?
additional information
?
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Substrates: VCPO Mcl24 from the merochlorin biosynthetic pathway shows an incredible ability to multitask, displaying all aforementioned VCPO function-alities (oxidative halogenation, terpene cyclization, and alpha-hydroxyketone rearrangement) within one enzyme. At pH 6.0, Mcl24 catalyzes the halogenation, oxidative dearomatization, and terpene cyclization of premerochlorin to generate two dominant monochlorinated merochlorins. These structurally divergent molecules arise due to the final terpene cyclization cascade ending with a carbon-carbon bond, or oxygen-carbon bond in merochlorins A and B, respectively. Under basic conditions (pH 8.0) the product distribution of Mcl24 is altered to predominantly catalyze the formation of merochlorin X, an alpha-hydroxyketone rearranged intermediate that may be further tailored by additional biosynthetic enzymes to generate merochlorins C and D. The major mechanistic difference during the biosyntheses of these molecules involves the addition of water to the oxidatively dearomatized molecule, which Mcl24 catalyzes more favorably at a basic pH. Hydration of the benzylic cation facilitates dichlorination and the corresponding rearrangement. in vitro, Mcl24 generates a large number of by-products because of the substantial oxidative instability of the premerochlorin substrate
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additional information
?
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Substrates: in the napyradiomycin suite of molecules, VCPO NapH1 catalyzes the chloronium-induced cyclization of the dimethylallyl (prenyl) side chain of naphthomevalin to generate the tricyclic compound napyradiomycin A1, e.g. coverting methylated naphthomevalin analogue SF2415B1 isolated from Streptomyces aculeolatus NRRL 18442 to 7-methyl-napyradiomycin A1 (SF2415B3). Incubation of NapH1 with SF2415B1 in the presence of bromide facilitated a product consistent with bromonium-induced cyclization, which is a naturally produced napyradiomycin analogue. NapH1 halogenation is diastereoselective at the newly formed stereocenter at the chlorine atom, implying a specific facial chloronium formation and cyclization by the adjacent hydroxy group. NapH1 also catalyzes analogous chlorination and cyclization reactions on the des-methylated SF2415B1 substrate naphthomevalin. But NapH1 fails to show any catalytic activity on the linear terpene alcohol precursor ()-nerolidol or the related meroterpenoid-like compound lapachol, highlighting the extreme selectivity NapH1 has for its requisite substrate. Reactions catalyzed by NapH1 are also stereoselective, evidenced by the single enantiomer of napyradiomycin A1 generated from the synthetic, racemic naphthomevalin substrate. The concomitant, unreacted naphthomevalin recovered from a NapH1 assay, shows an opposite circular dichroism spectrum to naphthomevalin naturally isolated from Streptomyces bacteria or that produced in vitro by NapH3 reaction
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additional information
?
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Substrates: meta-vanadate and ortho-vanadate, exhibits competitive inhibition of phytase, making it bifunctional to act as haloperoxidase. Molecular docking supports vanadate to share its binding site with substrate phytate, molecular docking study and inhibition mechanism, overview. The active site of haloperoxidase shows close similarity with histidine acid phytases. Inhibition of phytase by vanadate can make the enzyme behave as a vanadate-dependent haloperoxidase provided phosphoesterase activity of the enzyme is shut down by the vanadate. The vanadate exists as an anion at pH 3.0 and possibly binds to the active site cleft of phytase, which has a cluster of positively charged amino acids arginine, lysine, and histidine below the isoelectric point (pI) of the enzyme. Upon molecular docking of metavanadate with the rPPHY, it was observed to interact with the same amino acid residues of the catalytic site, with which substrate interacts. Both inhibitor and substrate might sit into the catalytic cleft of the enzyme which is placed between conserved alpha/beta-domain and a variable alpha-domain of rPPHY. When bonding of the substrate/inhibitor was analyzed, it is found to form bonds with arginine (R70), arginine (R74), and aspartate (D344). Inhibition kinetics of phytase by metavanadate. Inhibition of phytase by metavanadate suggests the applicability of rPPHY as haloperoxidase. The reaction is carried out with KBr, metavanadate, H2O2, and phenol red, while observed intermittently for change in color from red-orange to blue-violet
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-(2-amino-3-chlorophenyl)pyrrole + Cl- + H2O2
aminopyrrolnitrin + ?
-
Substrates: enzyme is involved in the biosynthesis of the antibiotic pyrrolnitrin
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?
pre-merochlorin + Cl- + H+ + H2O2
merochlorin A + merochlorin B + 2 H2O
Substrates: -
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?
RH + Cl- + H2O2 + H+
RCl + 2 H2O
Substrates: -
Products: -
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?
additional information
?
-
Substrates: repression by addition of glucose
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?
additional information
?
-
-
Substrates: repression by addition of glucose
Products: -
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?
additional information
?
-
Substrates: the enzyme may have a role in the natural production of high-molecular-weight chloroaromatics and in lignin breakdown
Products: -
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?
additional information
?
-
-
Substrates: the enzyme may have a role in the natural production of high-molecular-weight chloroaromatics and in lignin breakdown
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
vanadate cofactor
complex hydrogen bonding around the vanadate cofactor, Atoms-in-molecules (AIM) analysis
-
vanadate cofactor
the enzyme utilizes a vanadate prosthetic group to coordinate cosubstrate hydrogen peroxide, VHPOs perform a two-electron oxidation of electrophilic halides to generate a vanadium-bound hypohalous acid. This electrophilic halenium source can then react with electron-rich scaffolds, facilitating halogenation, cyclization, and hydration reactions
-
vanadate cofactor
the enzyme utilizes a vanadate prosthetic group to coordinate cosubstrate hydrogen peroxide, VHPOs perform a two-electron oxidation of electrophilic halides to generate a vanadium-bound hypohalous acid. This electrophilic halenium source can then react with electron-rich scaffolds, facilitating halogenation, cyclization, and hydration reactions
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
vanadate
Vanadium
vanadate
the vanadate cofactor changes its protonation from quadruply protonated at pH 6.3 to triply protonated at pH 7.3 to doubly protonated at pH 8.3. In the mutant P395D/L241V/T343A, the vanadate protonation is the same at pH 5.0 and 8.3, and the cofactor is doubly protonated
Vanadium
the vanadate binding pocket seems to form a very rigid frame stabilizing oxyanion binding
Vanadium
substitution of vanadate in the active site by phosphate leads to inactivation of the enzyme. Pervanadate is bound much more strongly to the enzyme than vanadate
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
Vanadium
required, electronic structure of the vanadate protonation states, overview
Vanadium
the active-site vanadium(V) ion is linked to the protein via a histidine residue. Vanadium is a spectator ion that does not change its oxidation state during the reaction mechanism but holds and positions the H2O2 substrate and guides its proton-relay steps through its oxo and hydroxo ligands
Vanadium
required, vanadium-dependent haloperoxidases (VHPOs) are not redox active at the vanadium metal center, remaining in the V5+ oxidation state, and thus do not require additional regeneration systems nor suffer oxidative inactivation during catalysis
Vanadium
required, vanadium-dependent haloperoxidases (VHPOs) are not redox active at the vanadium metal center, remaining in the V5+ oxidation state, and thus do not require additional regeneration systems nor suffer oxidative inactivation during catalysis
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Br-
inhibition of mutant enzyme S402A between pH 3.5 and 4.5: concentrations greater than 0.2 mM inhibit, between pH 5.0 and 5.5: concentrations above 0.5 mM inhibit, between pH 6.0 and 6.3: 0.5 mM does not inhibit the mutant enzyme
Cl-
pH 4.1: mixed type inhibition with respect to H2O2, pH 3.1: competitive inhibition
hydrazine
uncompetitive; uncompetitive inhibition, inhibition constant: 0.3 mM
hydroxylamine
competitive and uncompetitive inhibition; inhibits rVCPO both competitively and uncompetitively. The competitive inhibition constant: 0.04 mM, uncompetitive inhibition 0.08 mM
NO3-
pH 5.5: competitive inhibition of the chlorination reaction with respect to chloride, uncompetitive with respect to H2O2
azide
uncompetitive; uncompetitive inhibition, inhibition constant: 50 nM
phosphate
substitution of vanadate in the active site by phosphate leads to inactivation of the enzyme. Presence of H2O2 prevents inactivation by phosphate; substitution of vanadate in the active site by phosphate leads to inactivation. Presence of H2O2 prevents the inactivation
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Km-value for Cl- is pH-dependent whereas the Km-value for Br- is hardly pH-dependent
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
oxidation of 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
5.5
the wild type enzyme shows maximal activity at a pH of 5.5, but at pH of 7.7, its activity is decreased a 1000fold
6 - 8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 5.5
pH 3.5: about 70% of maximal activity, pH 5.5: about 45% of maximal activity
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