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Enzyme Nomenclature
Information on EC 1.14.99.52 - L-cysteinyl-L-histidinylsulfoxide synthase
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.14.99.52
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RECOMMENDED NAME
GeneOntology No.
L-cysteinyl-L-histidinylsulfoxide synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-histidine + L-cysteine + O2 = S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
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L-histidine + L-cysteine + O2 = S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
the enzyme catalysis follows an thiol-ene type mechanism, it catalyzes C-S bond formation through an OvoA generated L-cysteine thiyl radical that attacks the unsaturated imidazole ring of L-histidine, overview
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L-histidine + L-cysteine + O2 = S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
the catalytic mechanism proceeds via radical intermediate, oxidation of histidine is thermodynamically most favorable for the formation of a HisNdelta(-H). radical via a proton-coupled electron transfer process, only the ferrous peroxysulfur complexes are sufficiently powerful enough oxidants to generate a histidyl-derived radical, not the superoxo-complexes
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L-histidine + L-cysteine + O2 = S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
catalytic mechanism: C-S bond formation is initiated by formation of a histidyl sp2 radical, formation of a histidyl PI-radical, and electrophilic attack of the iron-coordinated cysteine sulfoxide on histidine. The enzyme OvoA oxidizes cysteine to access an iron(IV)-oxo state (a in Figure 2) which then mediates oxidative sulfurization of histidine
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L-histidine + L-cysteine + O2 = S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
catalytic mechanism: C-S bond formation is initiated by formation of a histidyl sp2 radical, formation of a histidyl PI-radical, and electrophilic attack of the iron-coordinated cysteine sulfoxide on histidine. The enzyme OvoA oxidizes cysteine to access an iron(IV)-oxo state which then mediates oxidative sulfurization of histidine
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L-histidine + L-cysteine + O2 = S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
catalytic mechanism: C-S bond formation is initiated by formation of a histidyl sp2 radical, formation of a histidyl PI-radical, and electrophilic attack of the iron-coordinated cysteine sulfoxide on histidine. The enzyme OvoA oxidizes cysteine to access an iron(IV)-oxo state (a in Figure 2) which then mediates oxidative sulfurization of histidine; the catalytic mechanism proceeds via radical intermediate, oxidation of histidine is thermodynamically most favorable for the formation of a HisNdelta(-H). radical via a proton-coupled electron transfer process, only the ferrous peroxysulfur complexes are sufficiently powerful enough oxidants to generate a histidyl-derived radical, not the superoxo-complexes; the enzyme catalysis follows an thiol-ene type mechanism, it catalyzes C-S bond formation through an OvoA generated L-cysteine thiyl radical that attacks the unsaturated imidazole ring of L-histidine, overview
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SYSTEMATIC NAME
IUBMB Comments
L-histidine,L-cysteine:oxygen [S-(L-histidin-5-yl)-L-cysteine S-oxide-forming]
Requires Fe2+ for activity. The enzyme participates in ovothiol biosynthesis. It also has some activity as EC 1.13.11.20, cysteine dioxygenase, and can perform the reaction of EC 1.14.99.50, gamma-glutamyl hercynylcysteine sulfoxide synthase, albeit with low activity [4].
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
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the two known sulfoxide synthases EgtB and OvoA distinguish themselves from each other by their substrate preferences and product C-S bond regioselectivity
evolution
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enzyme OvoA belongs to the 2-His-1-carboxylate catalytic triad type of mononuclear non-heme iron enzymes
evolution
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enzyme OvoA belongs to the 2-His-1-carboxylate catalytic triad type of mononuclear non-heme iron enzymes; the enzyme belongs to the sulfoxide synthases; the two known sulfoxide synthases EgtB and OvoA distinguish themselves from each other by their substrate preferences and product C-S bond regioselectivity
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malfunction
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mutation of the 2-His-1-carboxylate catalytic triad of the enzyme disrupts the cysteine dioxygenase activity
malfunction
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mutation of the 2-His-1-carboxylate catalytic triad of the enzyme disrupts the cysteine dioxygenase activity
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metabolism
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OvoA is an iron(II) dependent sulfoxide synthase which catalyzes the first step in ovothiol A biosynthesis
metabolism
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the enzyme is involved in the ergothioneine and ovothiol biosynthesis. Besides catalyzing the oxidative coupling between histidine and cysteine, enzyme OvoA can also catalyze a direct oxidative coupling between hercynine and cysteine, which can shorten the ergothioneine biosynthetic pathway by two steps, overview
metabolism
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OvoAis required in ovothiol biosynthesis catalyzing the oxidative coupling between histidine and cysteine
metabolism
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OvoA is an iron(II) dependent sulfoxide synthase which catalyzes the first step in ovothiol A biosynthesis; OvoAis required in ovothiol biosynthesis catalyzing the oxidative coupling between histidine and cysteine; the enzyme is involved in the ergothioneine and ovothiol biosynthesis. Besides catalyzing the oxidative coupling between histidine and cysteine, enzyme OvoA can also catalyze a direct oxidative coupling between hercynine and cysteine, which can shorten the ergothioneine biosynthetic pathway by two steps, overview; the enzyme is involved in the ovothiol biosynthesis
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physiological function
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the enzyme is the ovothiol biosynthetic enzyme, ovothiols are histidine-derived thiols
physiological function
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the enzyme is the ovothiol biosynthetic enzyme, ovothiols are histidine-derived thiols
physiological function
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ovothiol is proposed to be involved in H2O2 scavenging and facilitating the fertilization process
physiological function
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ovothiol is proposed to be involved in H2O2 scavenging and facilitating the fertilization process; the enzyme is the ovothiol biosynthetic enzyme, ovothiols are histidine-derived thiols
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additional information
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the enzyme requires coordination of iron(II) to an unusual iron-binding motif
additional information
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the enzyme requires coordination of iron(II) to an unusual iron-binding motif
additional information
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the enzyme requires coordination of iron(II) to an unusual iron-binding motif
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-fluoro-L-histidine + L-cysteine + O2
S-(2-fluoro-L-histidin-5-yl)-L-cysteine S-oxide + H2O
D-histidine + L-cysteine + O2
S-(D-histidin-5-yl)-L-cysteine S-oxide + S-(D-histidin-2-yl)-L-cysteine S-oxide + H2O
histamine + L-cysteine + O2
S-(histamin-5-yl)-L-cysteine S-oxide + H2O
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?
L-histidinamide + L-cysteine + O2
S-(L-histidinamide-5-yl)-L-cysteine S-oxide + H2O
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?
2-fluoro-L-histidine + L-cysteine + O2
S-(2-fluoro-L-histidin-5-yl)-L-cysteine S-oxide + H2O
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?
2-fluoro-L-histidine + L-cysteine + O2
S-(2-fluoro-L-histidin-5-yl)-L-cysteine S-oxide + H2O
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?
4-methylimidazole + L-cysteine + O2
? + H2O
very low activity
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?
4-methylimidazole + L-cysteine + O2
? + H2O
very low activity
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?
D-histidine + L-cysteine + O2
S-(D-histidin-5-yl)-L-cysteine S-oxide + S-(D-histidin-2-yl)-L-cysteine S-oxide + H2O
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the reaction product as a mixture of 63% 5-D-histidyl-L-cysteine sulfoxide and 37% 2-D-histidyl-L-cysteine sulfoxide
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?
D-histidine + L-cysteine + O2
S-(D-histidin-5-yl)-L-cysteine S-oxide + S-(D-histidin-2-yl)-L-cysteine S-oxide + H2O
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the reaction product as a mixture of 63% 5-D-histidyl-L-cysteine sulfoxide and 37% 2-D-histidyl-L-cysteine sulfoxide
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?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
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?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
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?
L-cysteine + O2
cysteine sulfinic acid + H2O
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oxidation of cysteine to cysteine sulfinic acid in presence of hercynine or L-histidine
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?
L-cysteine + O2
cysteine sulfinic acid + H2O
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oxidation of cysteine to cysteine sulfinic acid in presence of hercynine or L-histidine
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?
L-cysteine + O2
L-cystine + H2O
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oxidation of cysteine to cystine
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?
L-cysteine + O2
L-cystine + H2O
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oxidation of cysteine to cystine
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?
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
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?
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
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?
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
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evaluation of the mechanistic feasibility of the various possible iron-oxygen oxidants in the proton-coupled electron transfer process or the electron transfer process, overview
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?
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
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?
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
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?
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
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evaluation of the mechanistic feasibility of the various possible iron-oxygen oxidants in the proton-coupled electron transfer process or the electron transfer process, overview
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?
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
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?
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
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?
additional information
?
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besides catalyzing the four-electron oxidative coupling between histidine and cysteine, enzyme OvoA can also catalyze a direct oxidative coupling between hercynine and cysteine, which can shorten the ergothioneine biosynthetic pathway by two steps. Enzyme OvoA can also catalyze the reaction of egtB between hercynine and gamma-L-glutamyl-L-cysteine, EC 1.14.99.50
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additional information
?
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OvoA catalyzes efficient in vitro sulfurization of L-histidine, D-histidine, 2-fluoro-L-histidine and compounds other than amino acids. No activity with 4-bromoimidazole, 4(5)-(hydroxymethyl) imidazole, urocanic acid, N-alpha-acetyl-L-histidine, and carnosine, as well as 3-pyridin-2-ylalanine, 3-pyridin-3-ylalanine, 3-(2-thioxo-2,3-dihydro-1H-imidazol-4-yl)-L-alaninamide, 1-methylimidazole, 2,5-diiodo-L-histidine, 5-fluoro-L-histidine, 5-chloro-L-histidine, 5-bromo-L-histidine, and 5-iodo-L-histidine
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additional information
?
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OvoA substrate specificity and substrate binding pocket flexibility, NMR analysis, overview
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additional information
?
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the enzyme catalyzes the oxidative coupling between histidine and cysteine. It can also catalyze the oxidative coupling between hercynine and cysteine, yet with a different regioselectivity, NMR spectroscopic product analysis, overview. Enzyme OvoA can also catalyze the oxidation of cysteine to either cysteine sulfinic acid or cystine. OvoA-catalyzed reactions can be systematically modulated by a slight modification of one of its substrates, histidine
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additional information
?
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OvoA catalyzes efficient in vitro sulfurization of L-histidine, D-histidine, 2-fluoro-L-histidine and compounds other than amino acids. No activity with 4-bromoimidazole, 4(5)-(hydroxymethyl) imidazole, urocanic acid, N-alpha-acetyl-L-histidine, and carnosine, as well as 3-pyridin-2-ylalanine, 3-pyridin-3-ylalanine, 3-(2-thioxo-2,3-dihydro-1H-imidazol-4-yl)-L-alaninamide, 1-methylimidazole, 2,5-diiodo-L-histidine, 5-fluoro-L-histidine, 5-chloro-L-histidine, 5-bromo-L-histidine, and 5-iodo-L-histidine
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additional information
?
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besides catalyzing the four-electron oxidative coupling between histidine and cysteine, enzyme OvoA can also catalyze a direct oxidative coupling between hercynine and cysteine, which can shorten the ergothioneine biosynthetic pathway by two steps. Enzyme OvoA can also catalyze the reaction of egtB between hercynine and gamma-L-glutamyl-L-cysteine, EC 1.14.99.50
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additional information
?
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OvoA substrate specificity and substrate binding pocket flexibility, NMR analysis, overview
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additional information
?
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the enzyme catalyzes the oxidative coupling between histidine and cysteine. It can also catalyze the oxidative coupling between hercynine and cysteine, yet with a different regioselectivity, NMR spectroscopic product analysis, overview. Enzyme OvoA can also catalyze the oxidation of cysteine to either cysteine sulfinic acid or cystine. OvoA-catalyzed reactions can be systematically modulated by a slight modification of one of its substrates, histidine
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
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?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
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?
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
B2VFD8
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?
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
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-
-
-
?
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
B2VFD8
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-
?
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
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-
-
-
?
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
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?
additional information
?
-
-
besides catalyzing the four-electron oxidative coupling between histidine and cysteine, enzyme OvoA can also catalyze a direct oxidative coupling between hercynine and cysteine, which can shorten the ergothioneine biosynthetic pathway by two steps. Enzyme OvoA can also catalyze the reaction of egtB between hercynine and gamma-L-glutamyl-L-cysteine, EC 1.14.99.50
-
-
-
additional information
?
-
-
besides catalyzing the four-electron oxidative coupling between histidine and cysteine, enzyme OvoA can also catalyze a direct oxidative coupling between hercynine and cysteine, which can shorten the ergothioneine biosynthetic pathway by two steps. Enzyme OvoA can also catalyze the reaction of egtB between hercynine and gamma-L-glutamyl-L-cysteine, EC 1.14.99.50
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
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a mononuclear non-heme iron enzyme, iron-dependent enzyme, the molecular basis for iron recognition probably maps to a conserved HX3HXE motif in the N-terminal domains of both OvoA
Fe2+
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a mononuclear non-heme iron enzyme, dependent on, ligand with 2-His-1-carboxylate facial triad
Fe2+
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a mononuclear non-heme iron enzyme, iron-dependent enzyme, the molecular basis for iron recognition probably maps to a conserved HX3HXE motif in the N-terminal domains of both OvoA
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
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free-energy cost calculations for determining the catalytic mechanism, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
recombinant Strep-tagged enzyme from Escherichia coli by affinity chromatography
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recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
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recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene ovoA, recombinant expression of His-tagged enzyme in Escherichia coli
gene ovoA, the mutant enzyme loses the cysteine dioxygenase activity but also stops catalyzing the formation of oxidative coupling product
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gene ovoA, recombinant expression of His-tagged enzyme in Escherichia coli
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gene ovoA, recombinant expression of His-tagged enzyme in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E176A
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site-directed mutagenesis, the mutant shows reduced enzyme activity by at least 100fold compared to the wild-type enzyme
H170A
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site-directed mutagenesis, the mutant shows reduced enzyme activity by at least 100fold compared to the wild-type enzyme
H174A
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site-directed mutagenesis, the mutant shows reduced enzyme activity by at least 100fold compared to the wild-type enzyme
E176A
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site-directed mutagenesis, the mutant shows reduced enzyme activity by at least 100fold compared to the wild-type enzyme
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H170A
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site-directed mutagenesis, the mutant shows reduced enzyme activity by at least 100fold compared to the wild-type enzyme
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H174A
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site-directed mutagenesis, the mutant shows reduced enzyme activity by at least 100fold compared to the wild-type enzyme
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
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potential application of the oxidative coupling between hercynine and cysteine for industrial ergothioneine production
synthesis
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potential application of the oxidative coupling between hercynine and cysteine for industrial ergothioneine production
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.99.52)
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