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Information on EC 1.14.99.52 - L-cysteinyl-L-histidinylsulfoxide synthase
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1.14.99.52 L-cysteinyl-L-histidinylsulfoxide synthaseIUBMB Comments
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 .
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
plovoa, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5-histidylcysteine sulfoxide synthase
OvoA
OvoA-like protein
OvoAe
OvoA_1
OvoA_2
OvoA
-
-
-
-
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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
-
-
-
-
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
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
-
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
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
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
-
-
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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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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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
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
histamine + L-cysteine + O2
S-(histamin-5-yl)-L-cysteine S-oxide + H2O
-
-
-
?
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
-
-
-
?
4-methylimidazole + L-cysteine + O2
? + H2O
very low activity
-
-
?
4-methylimidazole + L-cysteine + O2
? + H2O
very low activity
-
-
?
D-histidine + L-cysteine + O2
S-(D-histidin-5-yl)-L-cysteine S-oxide + S-(D-histidin-2-yl)-L-cysteine S-oxide + H2O
-
the reaction product as a mixture of 63% 5-D-histidyl-L-cysteine sulfoxide and 37% 2-D-histidyl-L-cysteine sulfoxide
-
?
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
-
?
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
Moorena producens
-
-
-
?
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
Moorena producens PAL-8-15-08-1
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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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reaction of EC 1.14.99.51
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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
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
oxidation of cysteine to cysteine sulfinic acid in presence of hercynine or L-histidine
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?
L-cysteine + O2
L-cystine + H2O
oxidation of cysteine to cystine
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?
L-cysteine + O2
L-cystine + H2O
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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-
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?
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
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-
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?
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
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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OvoA modifies the C5 position of the imidazole ring of L-His, site selectivity of the transformation
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?
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
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-
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?
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
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
Moorena producens
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-
?
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
Moorena producens PAL-8-15-08-1
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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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-
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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
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-
?
additional information
?
-
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
?
-
OvoA substrate specificity and substrate binding pocket flexibility, NMR analysis, overview
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-
?
additional information
?
-
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
-
-
?
additional information
?
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-
OvoA in ovothiol biosynthesis is a mononuclear non-heme iron enzyme catalyzing the oxidative coupling between L-histidine and L-cysteine. It can also catalyze the oxidative coupling between hercynine and cysteine, yet with a different regioselectivity (cf. Ec 1.14.99.51). OvoA can also catalyze the oxidation of cysteine to either cysteine sulfinic acid or cystine, OvoA has cysteine dioxygenase activity (cf. EC 1.13.11.20). A 3-His catalytic triad is a prerequisite for the cysteine dioxygenase activity
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?
additional information
?
-
-
the ovothiol biosynthetic sulfoxide synthase OvoA from Erwinia tasmaniensis (OvoAErwin) is a promiscuous enzyme. This enzyme is most efficient in making its native product S-(L-histidin-5-yl)-L-cysteine S-oxide, but, when presented with N-alpha-trimethylhistidine as a sulfur acceptor, the enzyme switches product specificity and produces gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide albeit with significantly lower efficiency
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-
?
additional information
?
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OvoA incubated with hercynine (the normal substrate for EgtB, EC 1.14.99.50) and cysteine produces primarily cysteine sulfinic acid, the product of cysteine dioxygenase-type chemistry, cf. EC 1.13.11.20
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-
?
additional information
?
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the OvoA-catalyzed reactions can be systematically modulated by a slight modification of one of its substrates, L-histidine. Substrate specificity of OvoA, detailed overview
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-
?
additional information
?
-
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when OvoA's native substrate histidine is replaced by hercynine, OvoA can catalyze a one-step transformation reaction of hercynylcysteine S-oxide synthase, EC 1.14.99.51, resulting in kobs changes by 2fold for hercynine, while Km for cysteine increases from 0.3 mM to 3.19 mM. OvoA preferentially uses histidine and cysteine. OvoA also catalyzes the oxidation of cysteine to cysteine sulfinic acid, EC 1.13.11.20. Enzyme activity determination using : a 1H NMR assay of chemical shift of the imidazole hydrogen atoms
-
-
?
additional information
?
-
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
-
-
?
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
?
-
OvoA substrate specificity and substrate binding pocket flexibility, NMR analysis, overview
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
short cyanobacterial OvoA-type enzymes may contribute to ergothioneine (EC 1.14.99.51) instead of ovothiol production
-
-
?
additional information
?
-
Moorena producens
an OvoA-like protein, full-length OvoA homologue, OvoA_2, is a monofunctional sulfoxide synthase
-
-
?
additional information
?
-
Moorena producens
an OvoA-like protein, full-length OvoA homologue, OvoA_2, is a monofunctional sulfoxide synthase
-
-
?
additional information
?
-
Moorena producens
in a competitive reaction containing 1 mM of each histidine, N-alpha-trimethylhistidine, and cysteine, OvoAErwin produces only S-(L-histidin-5-yl)-L-cysteine S-oxide, whereas OvoAErw-NW and EgtB(ovo) produce exclusively gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide
-
-
?
additional information
?
-
Moorena producens
in a competitive reaction containing 1 mM of each histidine, N-alpha-trimethylhistidine, and cysteine, OvoAErwin produces only S-(L-histidin-5-yl)-L-cysteine S-oxide, whereas OvoAErw-NW and EgtB(ovo) produce exclusively gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide
-
-
?
additional information
?
-
Moorena producens PAL-8-15-08-1
an OvoA-like protein, full-length OvoA homologue, OvoA_2, is a monofunctional sulfoxide synthase
-
-
?
additional information
?
-
Moorena producens PAL-8-15-08-1
an OvoA-like protein, full-length OvoA homologue, OvoA_2, is a monofunctional sulfoxide synthase
-
-
?
additional information
?
-
Moorena producens PAL-8-15-08-1
in a competitive reaction containing 1 mM of each histidine, N-alpha-trimethylhistidine, and cysteine, OvoAErwin produces only S-(L-histidin-5-yl)-L-cysteine S-oxide, whereas OvoAErw-NW and EgtB(ovo) produce exclusively gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide
-
-
?
additional information
?
-
Moorena producens PAL-8-15-08-1
in a competitive reaction containing 1 mM of each histidine, N-alpha-trimethylhistidine, and cysteine, OvoAErwin produces only S-(L-histidin-5-yl)-L-cysteine S-oxide, whereas OvoAErw-NW and EgtB(ovo) produce exclusively gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide
-
-
?
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NATURAL SUBSTRATE
NATURAL 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
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
Moorena producens
-
-
-
?
hercynine + gamma-L-glutamyl-L-cysteine + O2
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
Moorena producens PAL-8-15-08-1
-
-
-
?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
reaction of EC 1.14.99.51
-
-
?
hercynine + L-cysteine + O2
S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
-
-
?
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
-
?
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
-
-
?
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
-
?
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
Moorena producens
-
-
-
?
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
Moorena producens PAL-8-15-08-1
-
-
-
?
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
-
?
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
-
?
L-histidine + L-cysteine + O2
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
-
-
-
?
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
?
-
-
OvoA in ovothiol biosynthesis is a mononuclear non-heme iron enzyme catalyzing the oxidative coupling between L-histidine and L-cysteine. It can also catalyze the oxidative coupling between hercynine and cysteine, yet with a different regioselectivity (cf. Ec 1.14.99.51). OvoA can also catalyze the oxidation of cysteine to either cysteine sulfinic acid or cystine, OvoA has cysteine dioxygenase activity (cf. EC 1.13.11.20). A 3-His catalytic triad is a prerequisite for the cysteine dioxygenase activity
-
-
?
additional information
?
-
-
the ovothiol biosynthetic sulfoxide synthase OvoA from Erwinia tasmaniensis (OvoAErwin) is a promiscuous enzyme. This enzyme is most efficient in making its native product S-(L-histidin-5-yl)-L-cysteine S-oxide, but, when presented with N-alpha-trimethylhistidine as a sulfur acceptor, the enzyme switches product specificity and produces gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide albeit with significantly lower efficiency
-
-
?
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
?
-
-
short cyanobacterial OvoA-type enzymes may contribute to ergothioneine (EC 1.14.99.51) instead of ovothiol production
-
-
?
additional information
?
-
Moorena producens
an OvoA-like protein, full-length OvoA homologue, OvoA_2, is a monofunctional sulfoxide synthase
-
-
?
additional information
?
-
Moorena producens
an OvoA-like protein, full-length OvoA homologue, OvoA_2, is a monofunctional sulfoxide synthase
-
-
?
additional information
?
-
Moorena producens PAL-8-15-08-1
an OvoA-like protein, full-length OvoA homologue, OvoA_2, is a monofunctional sulfoxide synthase
-
-
?
additional information
?
-
Moorena producens PAL-8-15-08-1
an OvoA-like protein, full-length OvoA homologue, OvoA_2, is a monofunctional sulfoxide synthase
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
a mononuclear non-heme iron enzyme, dependent on, ligand with 2-His-1-carboxylate facial triad
Fe2+
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+
-
non-heme iron, required for catalysis,residues in the HX3HXE motif might be involved in iron binding
Fe2+
required, the DinB superfamily domain contains the conserved HX3HXE putative iron-binding motif
Fe2+
-
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
D-isoascorbate
provides a nearly 100fold increase in enzyme activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene ovoA
UniProt
brenda
collected in the Gulf of Naples, near Castel dell'Ovo, from a location that is not privately-owned or protected in any way, and in collected at the Marine Protected Area Gaiola at station G1 in October of 2013
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
sea urchin Paracentrotus lividus eggs contain high concentrations (in the mM range) of ovothiol A
brenda
sea urchin Strongylocentrotus purpuratus eggs contain high concentrations (in the mM range) of ovothiol C
brenda
PlOvoA embryo expression significantly increased at the pluteus stage
brenda
additional information
enzyme expression analysis, PlOvoA expression profile and response to environmental stress conditions, overview. Ovothiol levels significantly increase at the prism stage after exposure to the metal, with respect to the control, whereas no significant increase is detected at the swimming blastula stage
brenda
additional information
-
enzyme expression analysis, PlOvoA expression profile and response to environmental stress conditions, overview. Ovothiol levels significantly increase at the prism stage after exposure to the metal, with respect to the control, whereas no significant increase is detected at the swimming blastula stage
brenda
additional information
enzyme expression analysis
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
enzyme OvoA belongs to the 2-His-1-carboxylate catalytic triad type of mononuclear non-heme iron enzymes
evolution
the two known sulfoxide synthases EgtB and OvoA distinguish themselves from each other by their substrate preferences and product C-S bond regioselectivity
evolution
-
cyanobacterial OvoA homologues (Egt-B(ovo)) have evolved to catalyze an EgtB-type reaction by convergent evolution, cf. EC 1.14.99.50, in a competitive reaction containing 1 mM of each histidine, N-alpha-trimethylhistidine, and cysteine, OvoAErw-NW and EgtB(ovo) produce exclusively gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide
evolution
Moorena producens
cyanobacterial OvoA homologues (Egt-B(ovo)) have evolved to catalyze an EgtB-type reaction by convergent evolution, cf. EC 1.14.99.50, in a competitive reaction containing 1 mM of each histidine, N-alpha-trimethylhistidine, and cysteine, OvoAErw-NW and EgtB(ovo) produce exclusively gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide
evolution
-
cyanobacterial OvoA homologues (Egt-B(ovo)) have evolved to catalyze an EgtB-type reaction by convergent evolution, cf. EC 1.14.99.50, in a competitive reaction containing 1 mM of each histidine, N-alpha-trimethylhistidine, and cysteine, OvoAErw-NW and EgtB(ovo) produce exclusively gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide. Because Erwinia tasmaniensis and most other OvoA encoding organisms do not encode an EgtD-type histidine methyltransferase, it seems clear that this N-alpha-trimethylhistidine-consuming side activity of OvoAErwin has no physiological purpose. Such promiscuity may have facilitated the transition of an ancestral sulfoxide synthase from ovothiol to erothioneine biosynthesis
evolution
-
OvoA and EgtB, EC 1.14.99.50, are related in sequence, while they are biochemically distinct
evolution
OvoA evolved in most marine metazoans and was lost in bony vertebrates during the transition from the aquatic to terrestrial environment. Evolutionary history of OvoA in metazoans, overview
evolution
OvoA evolved in most marine metazoans and was lost in bony vertebrates during the transition from the aquatic to terrestrial environment. The DinB superfamily domain contains the conserved HX3HXE putative iron-binding motif. The residues 581-587, 602-603, 661-663, and 680, considered to be involved in the formation of SAM-binding site, are conserved with the bacterial orthologous gene. OvoA shares two protein domains with EgtB, the DinB superfamily domain and the FGE-sulfatase domain but differs for the additional C-terminal putative SAM-transferase domain. Evolutionary history of OvoA in metazoans, overview
evolution
Moorena producens PAL-8-15-08-1
-
cyanobacterial OvoA homologues (Egt-B(ovo)) have evolved to catalyze an EgtB-type reaction by convergent evolution, cf. EC 1.14.99.50, in a competitive reaction containing 1 mM of each histidine, N-alpha-trimethylhistidine, and cysteine, OvoAErw-NW and EgtB(ovo) produce exclusively gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide
-
evolution
-
the two known sulfoxide synthases EgtB and OvoA distinguish themselves from each other by their substrate preferences and product C-S bond regioselectivity
-
evolution
-
enzyme OvoA belongs to the 2-His-1-carboxylate catalytic triad type of mononuclear non-heme iron enzymes
-
malfunction
mutation of the 2-His-1-carboxylate catalytic triad of the enzyme disrupts the cysteine dioxygenase activity
malfunction
-
mutation of any of the residues in the HX3HXE motif in OvoA results in an over 100fold attenuation of activity
malfunction
-
mutation of the 2-His-1-carboxylate catalytic triad of the enzyme disrupts the cysteine dioxygenase activity
-
metabolism
OvoA is an iron(II) dependent sulfoxide synthase which catalyzes the first step in ovothiol A biosynthesis
metabolism
OvoAis required in ovothiol biosynthesis catalyzing the oxidative coupling between histidine and cysteine
metabolism
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
-
enzyme OvoA is responsible for the oxidative C-S bond formation in ovothiol biosynthesis. OvoA in ovothiol biosynthesis has a relaxed substrate specificity
metabolism
gene ovoA is involved in ovothiol biosynthesis
metabolism
-
OvoA in ovothiol biosynthesis catalyzes the oxidative coupling between L-histidine and L-cysteine. It can also catalyze the oxidative coupling between hercynine and cysteine, yet with a different regioselectivity. OvoA can also catalyze the oxidation of cysteine to either cysteine sulfinic acid or cystine. Formation of S-(L-histidin-5-yl)-L-cysteine S-oxide and cysteine sulfinic acid might be two branching pathways in OvoA catalysis
metabolism
-
sulfoxide synthase OvoA catalyzes the formation of 5-histidylcysteine sulfoxide in the ovothiol biosynthesis. Short cyanobacterial OvoA-type enzymes may contribute to ergothioneine (EC 1.14.99.51) instead of ovothiol production
metabolism
Moorena producens
sulfoxide synthase OvoA catalyzes the formation of 5-histidylcysteine sulfoxide in the ovothiol biosynthesis. Short cyanobacterial OvoA-type enzymes may contribute to ergothioneine (EC 1.14.99.51) instead of ovothiol production
metabolism
-
sulfoxide synthase OvoA catalyzes the formation of 5-histidylcysteine sulfoxide in the ovothiol biosynthesis. Short cyanobacterial OvoA-type enzymes may contribute to ergothioneine (EC 1.14.99.51) instead of ovothiol production
metabolism
Moorena producens PAL-8-15-08-1
-
sulfoxide synthase OvoA catalyzes the formation of 5-histidylcysteine sulfoxide in the ovothiol biosynthesis. Short cyanobacterial OvoA-type enzymes may contribute to ergothioneine (EC 1.14.99.51) instead of ovothiol production
-
metabolism
-
OvoA is an iron(II) dependent sulfoxide synthase which catalyzes the first step in ovothiol A biosynthesis
-
metabolism
-
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
-
OvoAis required in ovothiol biosynthesis catalyzing the oxidative coupling between histidine and cysteine
-
physiological function
ovothiol is proposed to be involved in H2O2 scavenging and facilitating the fertilization process
physiological function
-
the enzyme is the ovothiol biosynthetic enzyme, ovothiols are histidine-derived thiols
physiological function
the enzyme is the ovothiol biosynthetic enzyme, ovothiols are histidine-derived thiols
physiological function
crucial role of OvoA in protecting embryos released in seawater from environmental cues, thus allowing the survival under different conditions
physiological function
-
the enzyme is the ovothiol biosynthetic enzyme, ovothiols are histidine-derived thiols
-
physiological function
-
ovothiol is proposed to be involved in H2O2 scavenging and facilitating the fertilization process
-
additional information
-
the enzyme requires coordination of iron(II) to an unusual iron-binding motif
additional information
the enzyme requires coordination of iron(II) to an unusual iron-binding motif
additional information
Moorena producens
an OvoA-like protein, full-length OvoA homologue, OvoA_1, with a C-terminal methyltransferase, most OvoAs contain a C-terminal methyltransferase
additional information
Moorena producens
an OvoA-like protein, full-length OvoA homologue, OvoA_1, with a C-terminal methyltransferase, most OvoAs contain a C-terminal methyltransferase
additional information
enzyme structure modeling, excluding the C-terminal additional domain, overview
additional information
-
enzyme structure modeling, excluding the C-terminal additional domain, overview
additional information
Moorena producens
homologue OvoA_2 is a monofunctional sulfoxide synthase without a C-terminal methyltransferase
additional information
Moorena producens
homologue OvoA_2 is a monofunctional sulfoxide synthase without a C-terminal methyltransferase
additional information
-
residues in the HX3HXE motif are catalytically important (i.e., likely bind iron). Structure homology modeling, overview
additional information
Moorena producens PAL-8-15-08-1
-
homologue OvoA_2 is a monofunctional sulfoxide synthase without a C-terminal methyltransferase
-
additional information
Moorena producens PAL-8-15-08-1
-
an OvoA-like protein, full-length OvoA homologue, OvoA_1, with a C-terminal methyltransferase, most OvoAs contain a C-terminal methyltransferase
-
additional information
-
the enzyme requires coordination of iron(II) to an unusual iron-binding motif
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A1D8U0C7_9CYAN
Moorena producens PAL-8-15-08-1
454
0
53007
TrEMBL
-
A0A1D8U386_9CYAN
Moorena producens PAL-8-15-08-1
717
0
81849
TrEMBL
-
B2VFD8_ERWT9
Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99)
719
0
82439
TrEMBL
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E176A
site-directed mutagenesis, the mutant shows reduced enzyme activity by at least 100fold compared to the wild-type enzyme
E176H
H170A
site-directed mutagenesis, the mutant shows reduced enzyme activity by at least 100fold compared to the wild-type enzyme
H174A
site-directed mutagenesis, the mutant shows reduced enzyme activity by at least 100fold compared to the wild-type enzyme