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1,1-dimethyl-4-chloro-3,5-cyclohexanedione + Cl- + H2O
?
-
-
-
?
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+
-
-
-
-
?
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+
-
-
-
-
?
4-(2-amino-3-chlorophenyl)pyrrole + Cl- + H2O2
aminopyrrolnitrin + ?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
Br- + H2O2 + H+
HOBr + H2O
Cl- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
i.e. monochlorodimedone
-
-
?
Cl- + H2O2 + H+
HOCl + H2O
cyclohexene + KBr + H2O2
2-bromocyclohexan-1-ol + 2 H2O
-
-
-
?
hept-1-ene + KBr + H2O2
1-bromoheptan-2-ol + 2 H2O
-
-
-
?
I- + H2O2 + H+
HOI + H2O
-
-
-
?
indole + Cl- + H2O2
oxindole + monochloroindole + H2O
methyl p-tolyl sulfide + H2O2
p-tolyl methyl sulfoxide
-
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-
-
-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
monochlorodimedone + Br- + H2O2
?
monochlorodimedone + Br- + H2O2
monobromo-monochlorodimedone + H2O
-
-
-
?
monochlorodimedone + bromide + H2O2 + H+
bromochlorodimedone + 2 H2O
-
-
-
?
monochlorodimedone + chloride + H2O2
dichlorodimedone + H2O
-
-
-
-
?
monochlorodimedone + chloride + H2O2 + H+
dichlorodimedone + H2O
-
-
-
?
monochlorodimedone + Cl- + H2O2
dichlorodimedone + H2O
-
-
-
?
pre-merochlorin + Cl- + H+ + H2O2
merochlorin A + merochlorin B + 2 H2O
-
-
-
?
RH + Br- + H2O2 + H+
RBr + 2 H2O
-
-
-
?
RH + Cl- + H2O2 + H+
RCl + 2 H2O
RH + I- + H2O2 + H+
RI + 2 H2O
-
-
-
?
styrene + KBr + H2O2
2-bromo-1-phenylethan-1-ol + 2-phenyloxirane + 2 H2O
-
-
-
?
styrene + KCl + H2O2
2-chloro-1-phenylethan-1-ol + 2 H2O
-
-
-
?
[(1E)-prop-1-en-1-yl]benzene + KBr + H2O2
(1R,2R)-2-bromo-1-phenylpropan-1-ol + 2 H2O
-
-
-
?
[(1Z)-prop-1-en-1-yl]benzene + KBr + H2O2
(1R,2S)-2-bromo-1-phenylpropan-1-ol + 2 H2O
-
-
-
?
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
-
chlorination in the pyrrole ring
-
?
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
-
chlorination in the pyrrole ring
-
?
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
-
chlorination in the pyrrole ring
-
?
4-(2-amino-3-chlorophenyl)pyrrole + Cl- + H2O2
aminopyrrolnitrin + ?
-
-
-
?
4-(2-amino-3-chlorophenyl)pyrrole + Cl- + H2O2
aminopyrrolnitrin + ?
-
enzyme is involved in the biosynthesis of the antibiotic pyrrolnitrin
-
?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
i.e. monochlorodimedone
-
-
?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
i.e. monochlorodimedone, brominating activity of chloroperoxidase
-
-
?
Br- + H2O2 + H+
HOBr + H2O
-
-
-
?
Br- + H2O2 + H+
HOBr + H2O
-
-
-
-
?
Cl- + H2O2 + H+
HOCl + H2O
-
-
-
?
Cl- + H2O2 + H+
HOCl + H2O
-
-
-
-
?
Cl- + H2O2 + H+
HOCl + H2O
-
-
-
?
indole + Br- + H2O2
?
-
-
-
-
?
indole + Br- + H2O2
?
-
-
-
-
?
indole + Cl- + H2O2
oxindole + monochloroindole + H2O
-
-
-
-
?
indole + Cl- + H2O2
oxindole + monochloroindole + H2O
-
-
-
?
indole + Cl- + H2O2
oxindole + monochloroindole + H2O
-
-
-
-
?
indole + Cl- + H2O2
oxindole + monochloroindole + H2O
-
-
-
-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
-
no activity
-
-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
-
-
-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
-
-
-
-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
-
-
-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
-
no activity
-
-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
-
no activity
-
-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
-
no activity
-
-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
-
no activity
-
-
?
monochlorodimedone + Br- + H2O2
?
-
-
-
-
?
monochlorodimedone + Br- + H2O2
?
-
-
-
?
monochlorodimedone + Br- + H2O2
?
-
-
-
-
?
monochlorodimedone + Br- + H2O2
?
-
-
-
-
?
monochlorodimedone + Br- + H2O2
?
-
-
-
-
?
monochlorodimedone + Br- + H2O2
?
-
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
-
-
?
monochlorodimedone + Br- + H2O2
?
-
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
-
-
?
RH + Cl- + H2O2 + H+
RCl + 2 H2O
-
-
-
?
RH + Cl- + H2O2 + H+
RCl + 2 H2O
-
-
-
?
RH + Cl- + H2O2 + H+
RCl + 2 H2O
-
-
-
?
RH + Cl- + H2O2 + H+
RCl + 2 H2O
-
-
-
?
1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane + Cl- + H2O2
additional information
-
-
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
-
-
-
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
?
-
-
no peroxidase activity, no catalase activity
-
-
?
additional information
?
-
oxidation of 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
additional information
?
-
-
oxidation of 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
additional information
?
-
repression by addition of glucose
-
-
?
additional information
?
-
-
repression by addition of glucose
-
-
?
additional information
?
-
the enzyme may have a role in the natural production of high-molecular-weight chloroaromatics and in lignin breakdown
-
-
?
additional information
?
-
the alkalophilic P395D/L241V/T343A mutant of vanadium chloroperoxidase shows bactericidal and virucidal activity
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
vanadium-dependent chloroperoxidases catalyze reactions involving peroxides and chloride, bromide, or iodide ions
-
-
-
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme may have a role in the natural production of high-molecular-weight chloroaromatics and in lignin breakdown
-
-
?
additional information
?
-
no substrates: geraniol and nerolidol or substrate analogues closely resembling the physiological substrate pre-merochlorin
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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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Burd, W.; Yourkevich, O.; Voskoboev, A.J.; van Pee, K.H.
Purification and properties of a non-haem chloroperoxidase from Serratia marcescens
FEMS Microbiol. Lett.
129
255-260
1995
Serratia marcescens
brenda
Baciocchi, E.; Fabbrini, M.; Lanzalunga, O.; Manduchi, L.; Pochetti, G.
Prochiral selectivity in H2O2-promoted oxidation of arylalkanols catalysed by chloroperoxidase: the role of the interactions between the OH group and the amino-acid residues in the enzyme active site
Eur. J. Biochem.
268
665-672
2001
Leptoxyphium fumago
brenda
ten Brink, H.B.; Dekker, H.L.; Schoemaker, H.E.; Wever, R.
Oxidation reactions catalyzed by vanadium chloroperoxidase from Curvularia inaequalis
J. Inorg. Biochem.
80
91-98
2000
Curvularia inaequalis (P49053), Curvularia inaequalis
brenda
Barnett, P.; Kruitbosch, D.L.; Hemrika, W.; Dekker, H.L.; Wever, R.
The regulation of the vanadium chloroperoxidase from Curvularia inaequalis
Biochim. Biophys. Acta
1352
73-84
1997
Curvularia inaequalis (P49053), Curvularia inaequalis
brenda
Bantleon, R.; Altenbuchner, J.; van Pee, K.H.
Chloroperoxidase from Streptomyces lividans: isolation and characterization of the enzyme and the corresponding gene
J. Bacteriol.
176
2339-2347
1994
Streptomyces lividans, Streptomyces lividans TK64
brenda
Renirie, R.; Hemrika, W.; Wever, R.
Peroxidase and phosphatase activity of active-site mutants of vanadium chloroperoxidase from the fungus Curvularia inaequalis. Implications for the catalytic mechanisms
J. Biol. Chem.
275
11650-11657
2000
Curvularia inaequalis (P49053), Curvularia inaequalis
brenda
Hemrika, W.; Renirie, R.; Macedo-Ribeiro, S.; Messerschmidt, A.; Wever, R.
Heterologous expression of the vanadium-containing chloroperoxidase from Curvularia inaequalis in Saccharomyces cerevisiae and site-directed mutagenesis of the active site residues His496, Lys353, Arg360, and Arg490
J. Biol. Chem.
274
23820-23827
1999
Curvularia inaequalis (P49053), Curvularia inaequalis
brenda
Simons, B.H.; Barnett, P.; Vollenbroek, E.G.M.; Dekker, H.L.; Muijsers, A.O.; Messerschmidt, A.; Wever, R.
Primary structure and characterization of the vanadium chloroperoxidase from the fungus Curvularia inaequalis
Eur. J. Biochem.
229
566-574
1995
Curvularia inaequalis (P49053), Curvularia inaequalis
brenda
Van Schijndel, J.W.; Barnett, P.; Roelse, J.; Vollenbroek, E.G.; Wever, R.
The stability and steady-state kinetics of vanadium chloroperoxidase from the fungus Curvularia inaequalis
Eur. J. Biochem.
225
151-157
1994
Curvularia inaequalis (P49053), Curvularia inaequalis
brenda
Pasta, P.; Carrea, G.; Colonna, S.; Gaggero, N.
Effects of chloride on the kinetics and stereochemistry of chloroperoxidase catalyzed oxidation of sulfides
Biochim. Biophys. Acta
1209
203-208
1994
Leptoxyphium fumago
brenda
Macedo-Ribeiro, S.; Hemrika, W.; Renirie, R.; Wever, R.; Messerschmidt, A.
X-ray crystal structures of active site mutants of the vanadium-containing chloroperoxidase from the fungus Curvularia inaequalis
J. Biol. Inorg. Chem.
4
209-219
1999
Curvularia inaequalis (P49053), Curvularia inaequalis
brenda
Wiesner, W.; van Pee, K.H.; Lingens, F.
Purification and characterization of a novel bacterial non-heme chloroperoxidase from Pseudomonas pyrrocinia
J. Biol. Chem.
263
13725-13732
1988
Burkholderia pyrrocinia
brenda
Bongs, G.; van Pee, K.H.
Enzymic chlorination using bacterial nonheme haloperoxidases
Enzyme Microb. Technol.
16
53-60
1993
Burkholderia pyrrocinia, Kitasatospora aureofaciens, Kitasatospora aureofaciens Tu24
-
brenda
Ortiz-Bermudez, P.; Srebotnik, E.; Hammel, K.E.
Chlorination and cleavage of lignin structures by fungal chloroperoxidases
Appl. Environ. Microbiol.
69
5015-5018
2003
Leptoxyphium fumago, Curvularia inaequalis (P49053)
brenda
Tanaka, N.; Hasan, Z.; Wever, R.
Kinetic characterization of active site mutants Ser402Ala and Phe397His of vanadium chloroperoxidase from the fungus Curvularia inaequalis
Inorg. Chim. Acta
356
288-296
2003
Curvularia inaequalis (P49053)
-
brenda
Tanaka, N.; Wever, R.
Inhibition of vanadium chloroperoxidase from the fungus Curvularia inaequalis by hydroxylamine, hydrazine and azide and inactivation by phosphate
J. Inorg. Biochem.
98
625-631
2004
Curvularia inaequalis (P49053), Curvularia inaequalis
brenda
Hasan, Z.; Renirie, R.; Kerkman, R.; Ruijssenaars, H.J.; Hartog, A.F.; Wever, R.
Laboratory-evolved vanadium chloroperoxidase exhibits 100-fold higher halogenating activity at alkaline pH: catalytic effects from first and second coordination sphere mutations
J. Biol. Chem.
281
9738-9744
2006
Curvularia inaequalis (P49053), Curvularia inaequalis
brenda
de Macedo-Ribeiro, S.; Renirie, R.; Wever, R.; Messerschmidt, A.
Crystal structure of a trapped phosphate intermediate in vanadium apochloroperoxidase catalyzing a dephosphorylation reaction
Biochemistry
47
929-934
2008
Curvularia inaequalis (P49053), Curvularia inaequalis
brenda
Renirie, R.; Dewilde, A.; Pierlot, C.; Wever, R.; Hober, D.; Aubry, J.M.
Bactericidal and virucidal activity of the alkalophilic P395D/L241V/T343A mutant of vanadium chloroperoxidase
J. Appl. Microbiol.
105
264-270
2008
Curvularia inaequalis (P49053)
brenda
Zhang, Y.; Gascon, J.A.
QM/MM investigation of structure and spectroscopic properties of a vanadium-containing peroxidase
J. Inorg. Biochem.
102
1684-1690
2008
Curvularia inaequalis (P49053)
brenda
Hoogenkamp, M.A.; Crielaard, W.; ten Cate, J.M.; Wever, R.; Hartog, A.F.; Renirie, R.
Antimicrobial activity of vanadium chloroperoxidase on planktonic Streptococcus mutans cells and Streptococcus mutans biofilms
Caries Res.
43
334-338
2009
Curvularia inaequalis (P49053)
brenda
Winter, J.; Moore, B.
Exploring the chemistry and biology of vanadium-dependent haloperoxidases
J. Biol. Chem.
284
18577-18581
2009
Curvularia inaequalis (P49053), Alternaria didymospora (P79087)
brenda
Geethalakshmi, K.R.; Waller, M.P.; Thiel, W.; Buehl, M.
51V NMR chemical shifts calculated from QM/MM models of peroxo forms of vanadium haloperoxidases
J. Phys. Chem. B
113
4456-4465
2009
Curvularia inaequalis (P49053)
brenda
Renirie, R.; Charnock, J.M.; Garner, C.D.; Wever, R.
Vanadium K-edge XAS studies on the native and peroxo-forms of vanadium chloroperoxidase from Curvularia inaequalis
J. Inorg. Biochem.
104
657-664
2010
Curvularia inaequalis (P49053), Curvularia inaequalis
brenda
Renirie, R.; Pierlot, C.; Wever, R.; Aubry, J.
Singlet oxygenation in microemulsion catalysed by vanadium chloroperoxidase
J. Mol. Catal. B
56
259-264
2009
Curvularia inaequalis (P49053)
-
brenda
Bernhardt, P.; Okino, T.; Winter, J.M.; Miyanaga, A.; Moore, B.S.
A stereoselective vanadium-dependent chloroperoxidase in bacterial antibiotic biosynthesis
J. Am. Chem. Soc.
133
4268-4270
2011
Streptomyces sp.
brenda
Persoon, I.F.; Hoogenkamp, M.A.; Bury, A.; Wesselink, P.R.; Hartog, A.F.; Wever, R.; Crielaard, W.
Antimicrobial effect of a modified vanadium chloroperoxidase on Enterococcus faecalis biofilms at root canal pH
J. Endod.
39
1035-1038
2013
Curvularia inaequalis (P49053)
brenda
Diethelm, S.; Teufel, R.; Kaysser, L.; Moore, B.S.
A multitasking vanadium-dependent chloroperoxidase as an inspiration for the chemical synthesis of the merochlorins
Angew. Chem. Int. Ed. Engl.
53
11023-11026
2014
Streptomyces sp. CNH189 (M4TL26)
brenda
Dong, J.J.; Fernandez-Fueyo, E.; Li, J.; Guo, Z.; Renirie, R.; Wever, R.; Hollmann, F.
Halofunctionalization of alkenes by vanadium chloroperoxidase from Curvularia inaequalis
Chem. Commun. (Camb.)
53
6207-6210
2017
Curvularia inaequalis (P49053), Curvularia inaequalis
brenda
Gupta, R.; Hou, G.; Renirie, R.; Wever, R.; Polenova, T.
51V NMR crystallography of vanadium chloroperoxidase and its directed evolution P395D/L241V/T343A mutant protonation environments of the active site
J. Am. Chem. Soc.
137
5618-5628
2015
Curvularia inaequalis (P49053)
brenda
Joshi, S.; Satyanarayana, T.
Characteristics and applicability of phytase of the yeast Pichia anomala in synthesizing haloperoxidase
Appl. Biochem. Biotechnol.
176
1351-1369
2015
Wickerhamomyces anomalus (D3HIF3)
brenda
Mubarak, M.; Gerard, E.; Blanford, C.; Hay, S.; De Visser, S.
How do vanadium chloroperoxidases generate hypochlorite from hydrogen peroxide and chloride? A computational study
ACS Catal.
10
14067-14079
2020
Curvularia inaequalis (P49053)
-
brenda
McLauchlan, C.C.; Murakami, H.A.; Wallace, C.A.; Crans, D.C.
Coordination environment changes of the vanadium in vanadium-dependent haloperoxidase enzymes
J. Inorg. Biochem.
186
267-279
2018
Curvularia inaequalis (P49053)
brenda
Anderson, G.A.; Behera, R.N.; Gomatam, R.
Calculation of higher protonation states and of a new resting state for vanadium chloroperoxidase using QM/MM, with an atom-in-molecules analysis
J. Mol. Graph. Model.
99
107624
2020
Curvularia inaequalis (P49053)
brenda
McKinnie, S.M.K.; Miles, Z.D.; Moore, B.S.
Characterization and biochemical assays of Streptomyces vanadium-dependent chloroperoxidases
Methods Enzymol.
604
405-424
2018
Streptomyces sp. CNQ-525 (A7KH27), Streptomyces sp. CNH189 (M4TL26)
brenda