Information on EC 1.11.1.18 - bromide peroxidase

Word Map on EC 1.11.1.18
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.11.1.18
-
RECOMMENDED NAME
GeneOntology No.
bromide peroxidase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
RH + HBr + H2O2 = RBr + 2 H2O
show the reaction diagram
Brings about the bromination of a range of organic molecules, forming stable C-Br bonds. Can also act on iodide ions. The enzymes of this group contain vanadium (V) bound to the active centre. Since the actual halogenating agents are the respective hypohalous acids, vanadium-containing halide peroxidases lack substrate specificity and regioselectivity.
-
-
-
SYSTEMATIC NAME
IUBMB Comments
bromide:hydrogen-peroxide oxidoreductase
Bromoperoxidases of red and brown marine algae (Rhodophyta and Phaeophyta) contain vanadate. They catalyse the bromination of a range of organic molecules such as sesquiterpenes, forming stable C-Br bonds. Bromoperoxidases also oxidize iodides.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
Doty
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain T 6
-
-
Manually annotated by BRENDA team
strain T 6
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Br- + H2O2 + (3R)-3-bromo-2,6-dimethylhept-5-en-2-ol
3,5-dibromo-2,6-dimethylheptane-2,6-diol + H2O
show the reaction diagram
-
-
70% yield, at pH 6.0
-
?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
show the reaction diagram
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
bromochlorodimedone + ?
show the reaction diagram
-
i.e. monochlorodimedone
-
-
?
Br- + H2O2 + 1-methoxynaphthalene
1-methoxy-4-bromonaphthalene + H2O
show the reaction diagram
-
-
-
-
?
Br- + H2O2 + 1-phenylpent-4-en-1-ol
4-bromo-1-phenylpentane-1,5-diol + 5-bromo-1-phenylpentane-1,4-diol + 2-(bromomethyl)-5-phenyltetrahydrofuran + H2O
show the reaction diagram
-
-
30% yield of 4-bromo-1-phenylpentane-1,5-diol, 28% yield of 5-bromo-1-phenylpentane-1,4-diol, and 25% yield of 2-(bromomethyl)-5-phenyltetrahydrofuran, at pH 6.0
-
?
Br- + H2O2 + 2,4,6-tribromophenol
1,3,6,8-tetrabromodibenzo-p-dioxin
show the reaction diagram
-
-
formation of ppb-level yields of 1,3,6,8-tetrabromodibenzo-p-dioxin through direct condensation. Additionally, 1,3,7,9-tetrabromodibenzo-p-dioxin, 1,2,4,7-tetrabromodibenzo-p-dioxin, and/or 1,2,4,8-tetrabromodibenzo-p-dioxin and 1,3,7-tribromodibenzo-p-dioxin and 1,3,8-tribromodibenzo-p-dioxin are frequently formed but at lower yields. Reaction probably proceeds via bromine shifts or Smiles rearrangements, whereas the tribromodibenzo-p-dioxins may result from subsequent debromination processes
-
?
Br- + H2O2 + 2-hydroxybenzyl alcohol
2,4,6-tribromophenol + H2O
show the reaction diagram
-
-
-
-
?
Br- + H2O2 + 2-methoxyphenol
2-bromo-6-methoxyphenol + 4-bromo-6-methoxyphenol + H2O
show the reaction diagram
-
56% of product, in a 21/79 mixture of o-/p-regioisomers, plus 10% 2,4-dibromo-6-methoxyphenol
-
?
Br- + H2O2 + 2-methylphenol
2-bromo-6-methylphenol + 4-bromo-6-methylphenol + H2O
show the reaction diagram
-
68% of product, in a 16/84 mixture of o-/p-regioisomers, plus 4% 2,4-dibromophenol
-
?
Br- + H2O2 + 2-t-butylphenol
2-bromo-6-t-butylphenol + 4-bromo-6-t-butylphenol + H2O
show the reaction diagram
-
42% of product, in a 36/64 mixture of o-/p-regioisomers, plus 2% 2,4-dibromo-6-t-butylphenol
-
?
Br- + H2O2 + 4-pentynoic acid
(5E)-bromomethylidenetetrahydro-2-furanone
show the reaction diagram
-
catalyzes the bromolactonization of 4-pentynoic acid forming (5E)-bromomethylidenetetrahydro-2-furanone. Formation of the bromofuranone likely results from an initial bromination reaction at the terminal alkyne, followed by cyclization from intermolecular nucleophilic attack by the terminal hydroxyl group
-
-
?
Br- + H2O2 + 5-methyl-1-phenylhex-4-en-1-ol
4-bromo-5-methyl-1-phenylhexane-1,5-diol + 2-(1-bromo-1-methylethyl)-5-phenyltetrahydrofuran + 3-bromo-2,2-dimethyl-6-phenyltetrahydro-2H-pyran + H2O
show the reaction diagram
-
-
69% yield of 4-bromo-5-methyl-1-phenylhexane-1,5-diol, 6% yield of 2-(1-bromo-1-methylethyl)-5-phenyltetrahydrofuran, and 9% yield of 3-bromo-2,2-dimethyl-6-phenyltetrahydro-2H-pyran, at pH 6.0
-
?
Br- + H2O2 + aniline
o-bromoaniline + p-bromoaniline + ?
show the reaction diagram
Br- + H2O2 + anisole
p-bromoanisole + o-bromoanisole + H2O
show the reaction diagram
-
-
-
-
?
Br- + H2O2 + cyclohexene
trans-1-hydroxy-2-bromocyclohexane
show the reaction diagram
-
-
-
-
?
Br- + H2O2 + cytidine
5-bromocytidine + H2O
show the reaction diagram
-
-
-
-
?
Br- + H2O2 + cytosine
5-bromocytosine + H2O
show the reaction diagram
-
-
-
-
?
Br- + H2O2 + methyl pyrrole-2-carboxylate
methyl 4-bromo-1H-pyrrole-2-carboxylate + methyl 5-bromo-1H-pyrrole-2-carboxylate + H2O
show the reaction diagram
-
-
quantitative conversion within 24 h, 94% of product in 93/7 ratio of 4-/5-substituted regioisomers
-
?
Br- + H2O2 + methyl pyrrole-2-carboxylate
methyl 5-amino-4-bromocyclopenta-1,3-diene-1-carboxylate + methyl 5-amino-3-bromocyclopenta-1,3-diene-1-carboxylate + methyl 5-amino-3,4-dibromocyclopenta-1,3-diene-1-carboxylate + H2O
show the reaction diagram
-
-
5% yield of methyl 5-amino-4-bromocyclopenta-1,3-diene-1-carboxylate, 59% yield of methyl 5-amino-3-bromocyclopenta-1,3-diene-1-carboxylate, and 5% yield of methyl 5-amino-3,4-dibromocyclopenta-1,3-diene-1-carboxylate, at pH 6.3 and 25C
-
?
Br- + H2O2 + monochlorodimedon
?
show the reaction diagram
-
-
-
?
Br- + H2O2 + monochlorodimedone
?
show the reaction diagram
-
-
-
-
?
Br- + H2O2 + monochlorodimedone
? + H2O
show the reaction diagram
Br- + H2O2 + monochlorodimedone
H2O + ?
show the reaction diagram
-
-
-
-
?
Br- + H2O2 + phenol
2,4,6-tribromophenol + H2O
show the reaction diagram
-
-
-
-
?
Br- + H2O2 + phenol
2-bromophenol + 4-bromophenol + H2O
show the reaction diagram
-
69% of product, in a 91/9 mixture of o-/p-regioisomers, plus 3% 2,4-dibromo-6-methylphenol and some 2,4,6-tribromophenol
-
?
Br- + H2O2 + phenol red
phenol blue + ?
show the reaction diagram
-
-
-
-
?
Br- + H2O2 + pyrazole
4-bromopyrazole + H2O
show the reaction diagram
-
-
-
-
?
Br- + H2O2 + styrene
DL-1 -bromo-2-hydroxy-2-phenylethane + H2O
show the reaction diagram
-
-
-
-
?
Br- + H2O2 + thiophene
2-bromothiophene + H2O
show the reaction diagram
-
-
-
-
?
Br- + H2O2 + trans-cinnamic acid
(+/-)-erythro-2-bromo-3-hydroxy-3-phenylpropionic acid + H2O
show the reaction diagram
-
-
-
-
?
Br- + H2O2 + trans-cinnamyl alcohol
(+/-)-1,3-dihydroxy-2-bromo-3-phenylpropane + H2O
show the reaction diagram
-
-
-
-
?
Br- + H2O2 + uracil
5-bromouracil + H2O
show the reaction diagram
-
-
-
-
?
Capso + Br- + peracetic acid
?
show the reaction diagram
cytosine + Br- + peracetic acid
5-bromocytosine + ?
show the reaction diagram
Hepes + Br- + peracetic acid
?
show the reaction diagram
I- + H2O2
triiodide + ?
show the reaction diagram
I- + H2O2 + monochlorodimedone
? + H2O
show the reaction diagram
-
-
-
?
I- + H2O2 + pyrazole
4-iodopyrazole + H2O
show the reaction diagram
-
-
-
-
?
I- + H2O2 + uracil
5-iodouracil + H2O
show the reaction diagram
-
-
-
-
?
monochlorodimedone + Br- + H2O2
?
show the reaction diagram
Mops + Br- + peracetic acid
5-bromocytosine + ?
show the reaction diagram
phenol + H2O2 + Br-
4-bromophenol + 2-bromophenol + H2O
show the reaction diagram
-
-
4-bromophenol + 2-bromophenol at the ratio of 4:1
-
?
taurine + Br- + peracetic acid
bromotaurine + ?
show the reaction diagram
Tes + Br- + peracetic acid
?
show the reaction diagram
Tris + Br- + peracetic acid
?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
activates
Co2+
-
activates
Cu2+
-
activates
Mg2+
-
activates
Mn2+
-
activates
Ni2+
-
activates
vanadate
in the solid state structure, every protein monomer binds one vanadate to the tele imidazole nitrogen of residue His486. In solutions of sodium orthovanadate, isoform apobromoperoxidase II recovers bromoperoxidase activity by one order of magnitude faster than apobromoperoxidase I
Vanadium
Zn2+
-
activates
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-Amino-1,2,4-triazole
-
45% inhibition at 5 mM, 90% inhibition at 40 mM
arsenate
-
competitive inhibitor
hydroxylamine
-
0.05 mM, 50% inhibition of brominating activity
phosphate
-
competitive inhibitor
potassium cyanide
-
0.05 mM, complete inhibition of bromoperoxidase-catalase activity
Sodium azide
-
0.05 mM, complete inhibition of bromoperoxidase-catalase activity
additional information
-
not inhibited by azide or cyanide. Excess bromide or chloride has no effect on its brominating activity
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetonitrile
-
sVBPO showed an increase in activity in the presence of acetonitrile, which is not observed with nVBPO or rVBPO
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002 - 0.021
1,1-dimethyl-4-chloro-3,5-cyclohexanedione
0.001 - 160
Br-
0.017 - 430
H2O2
0.08 - 33
I-
0.00012
monochlorodimedone
-
pH 6, 25C
additional information
additional information
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12
arsenate
-
-
0.06
phosphate
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.1
-
nonhaem-type bromoperoxidase BPO3
1.77
-
bromoperoxidase activity
9.9
-
crude extract, pH and temperature not specified in the publication
310
-
after 27fold purification, pH and temperature not specified in the publication
963
-
catalase activity
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.3
-
the pH optimum is independent of H2O2 and KBr when concentrations ranging from 5 to 100 mM
4.75
-
bromination of 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
5.5
-
1 mM sodium acetate buffer, BPO 1
6 - 6.5
-
maximum bromoperoxidase activity of mutant H480A under conditions of high substrate concentrations (5 mM H2O2 and 100 mM Br-), however with reduced specific activity as compared to recombinant wild-type enzyme
6
-
optimal bromoperoxidase activity of recombinant wild-type enzyme using low substrate concentrations (0.5 mM H2O2, 5 mM Br-) and high substrate concentrations (5 mM H2O2, 100 mM Br-)
6 - 7
-
dioxygen formation
6.5 - 7
-
dioxygen formation
6.5
-
MES buffer
7
-
rVBPO and nVBPO
7 - 8.5
-
catalase activity
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7
-
pH 5.0: about 35% of maximal activity, pH 7.0: about 25% of maximal activity
5.5 - 10
-
pH 5.5: 70-90% of maximal activity depending on enzyme form, pH 10.0: about 40% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
nonhaem-type bromoperoxidase BPO 1a
60
-
nonhaem-type bromoperoxidase BPO3
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45 - 75
-
45C: about 50% of maximal activity, 75C: about 60% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.6
-
isoelectric focusing, pH-range 3.5-9.5, nonhaem-type bromoperoxidase BPO 3
4.6
-
isoelectric focusing, pH-range 3.5-9.5, nonhaem-type bromoperoxidase BPO 1a
4.7
-
isoelectric focusing, pH-range 3.5-9.5, nonhaem-type bromoperoxidase BPO 1b
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
the lowest specific bromoperoxidase activity occurs during the midexponential phase of growth and then increases steeply during the late stationary phase
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31400
estimated from SDS-PAGE
32000
-
2 * 32000, SDS-PAGE
43000
-
2 * 43000, SDS-PAGE, nonhaem-type bromoperoxidase BPO 1b
54200
-
x * 54200, calculated from sequence
61000
-
2 * 61000, SDS-PAGE
65458
-
x * 65458, calculated
67400
2 * 67400, calculated, 2 * 64200-65000, MALDI-TOF
70000
-
gel filtration, nonhaem-type bromoperoxidase BPO 1a
74000
-
x * 74000, SDS-PAGE
83000
-
x * 83000, SDS-PAGE
84000
x * 84000, SDS-PAGE, recombinant protein with His-tag
97000
-
ultracentrifugation
127000 - 136000
-
gel filtration
127700 - 130000
MALDI-TOF
136000
gel filtration
740000
-
meniscus-depletion sedimentation equilibrium
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
-
12 * 64000, SDS-PAGE
homodimer
-
-
trimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystallized from ammonium sulfate solutions in a form suitable for X-ray diffraction analysis. Crystals are grown by the vapour-diffusion technique using the sitting-drop method. X-ray diffraction studies show that the crystals belong to the tetragonal space group P4(1)2(1)2 or P4(3)2(1)2 with a = b = 114.3 and c = 276.0 A. The crystals diffract to at least 2.4 A resolution
-
structure of the enzyme is solved by single isomorphous replacement anomalous scattering X-ray crystallography at 2.0 A resolution. Crystals of the holoenzyme and the apoenzyme are obtained from 2.1 M ammonium sulfate solutions buffered at pH 8.3 and diffract to 2.4 A resolution. The crystals are stable in the X-ray beam for more than one week. They belong to the tetragonal system, space group P4(3)2(1)2, with lattice constants a ?= 114.3 A,? c = 276.0 A
-
the crystals exhibit a teardrop morphology and are grown from 2 M ammonium dihydrogen phosphate pH and diffract to beyond 1.7 A resolution. They are in tetragonal space group P4222 with unit-cell dimensions of a = b = 201.9 A, c = 178.19 A, alpha = beta = gamma = 90
-
sitting drop vapour diffusion method, two crystal forms are obtained, one hexagonal form using ammonium phosphate as precipitant (form 1) and a second cubic vanadium bound form (form 2). The best crystals of the cubic form 2 containing vanadate are only obtained with the wild type enzyme. The optimised conditions use an initial protein concentration of 18 mg/ml in 50 mM Tris-H2SO4, 0.4 M KBr, 1 mM Na3VO4, 20% (w/v) polyethylene glycol 6000. For the wild type enzyme crystals grown in form 2, a mother liquor substituting the precipitant with 25% polyethylene glycol 400 and 25% polyethylene glycol 6000 is used
-
the hanging-drop vapor diffusion method
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
activity remains constant for at least 4 h
57
-
20 min, 50% loss of activity, enzyme preincubated without metal ion
65
-
20 min, recombinantly expressed enzyme is stable, native enzyme is completely inactivated
72
-
Tm-value
75
-
20 min, 50% loss of activity, enzyme preincubated with 1 mM vanadate
87
-
20 min, 50% loss of activity, enzyme preincubated with 1 mM Ca2+
92
-
20 min, 50% loss of activity, enzyme preincubated with 1 mM Ca2+ and 1 mM vanadium
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activity half-life times increase along the series of buffers: phosphate
-
after treatment with a mixture of chloroform/ethanol the enzyme still shows 65% of its initial brominating activity
-
Ca2+ significantly increased the enzyme stability. Strontium and magnesium ions have similar effects
-
circular dichroism measurements showed that the secondary structure is not affected upon incubation in 4% SDS
-
denaturation did not occur upon incubation in 4 M guanidine hydrochloride
-
dialysis of the enzyme preparation against 1 mM EDTA in 0.1 M citrate-phosphate buffer (pH 3.8) results in loss of enzymic activity. Incubation with vanadium, does not restore the enzymic activity. Also various other metal ions: Zn(II), Fe(II), Cu(II) and Mn(II) are ineffective in the reactivation of the preparation
-
vanadate increases the thermostability
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1-propanol
-
completely intact in the presence of 50% methanol
Ethanol
-
completely intact in the presence of 50% methanol
Methanol
-
completely intact in the presence of 50% methanol
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
20C, in 0.001 mM H2O2-incubated, MES-buffered (pH 6.22) aqueous alcoholic solution, half-life time of about 60 days
-
20C, in 0.001 mM NaCl-incubated, MES-buffered (pH 6.22) aqueous alcoholic solution, half-life time of about 24 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
isolation of three forms of CoVBPO: nVBPO which is isolated directly from the algal species, sVBPO which is produced in a soluble form by Escherichia coli and rVBPO which is expressed by Escherichia coli as inclusion bodies and subsequently refolded
-
Na3VO4 is added to the crude extract (1.12 mg protein/ml) followed by heat treatment at 70C for 2 h, 30-55% (w/v) ammonium sulfate precipitation and DEAE-52column chromatography
-
Ni2+-charged HiTrap chelating column chromatography
nonhaem-type bromoperoxidase BPO1a; nonhaem-type bromoperoxidase BPO1b; nonhaem-type bromoperoxidase BPO3
-
phenyl Sepharose column chromatography and Phenyl Sepharose gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme is overproduced in Streptomyces lividans TK64, up to 30000 times compared to Streptomyces aureofaciens
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
-
expression in Escherichia coli. Recombinant enzyme and its mutants have no enzyme activities, unless they are activated by Na3VO4
expression in Saccharomyces cerevisiae
-
overexpressed in Escherichia coli. The enzyme is found to be predominantly in the form of inclusion bodies
-
the gene is cloned in the positive selection vector pIJ699 and expression in Streptomyces lividans TK64. The cloned bromoperoxidase is overproduced up to 2800fold by the Streptomyces lividans transformant
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transcript abundance is relatively higher in seaweed samples treated with 50 parts per thousand artificial seawater compared to those treated in 10 and 30 parts per thousand artificial seawater
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H480A
-
results in the loss of the ability to efficiently oxidize bromide, but retains the ability to oxidize iodide
R397W
-
the mutant shows a different behaviour on bromide binding compared to the wild type enzyme, (the bromide is missing the hydrogen-binding interaction that held it in the active site of the wild type enzyme)
R379F
increase in affinity for Br-, enables the mutant to oxidize Cl-, decrease in affinity for I-
R379H
decrease in affinity for Br-
D229A
-
inactive mutant protein
H258Q
-
inactive mutant protein
S97A
-
inactive mutant protein
S97C
-
mutant with very low residual activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
-
immobilization of enzyme on magnetic micrometre-sized particles in quantitative yields, with up to 40% retention of initial bromoperoxidase activity. The immobilized enzyme is stable with a half-life time of about 160 days. It serves as reusable catalyst for bromide oxidation with H2O2 in up to 14 consecutive experiments. Immobilized enzyme is used for methyl pyrrole-2-carboxylate conversion into derivatives of naturally occurring compounds e.g. from Agelas oroides with product selectivity of up to 75%
Show AA Sequence (215 entries)
Please use the Sequence Search for a specific query.