1.14.99.52: L-cysteinyl-L-histidinylsulfoxide synthase
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For detailed information about L-cysteinyl-L-histidinylsulfoxide synthase, go to the full flat file.
Reaction
Synonyms
5-histidylcysteine sulfoxide synthase, OvoA, OvoA-like protein, OvoAe, OvoAErwin, OvoAt, OvoA_1, OvoA_2, PlOvoA, short OvoA homologue, SpOvoA, sulfoxide synthase
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General Information
General Information on EC 1.14.99.52 - L-cysteinyl-L-histidinylsulfoxide synthase
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evolution
malfunction
metabolism
physiological function
additional information
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
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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
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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
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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
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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
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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
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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 any of the residues in the HX3HXE motif in OvoA results in an over 100fold attenuation of 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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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
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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
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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
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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
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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
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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
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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
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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
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metabolism
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OvoAis required in ovothiol biosynthesis catalyzing the oxidative coupling between histidine and cysteine
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ovothiol is proposed to be involved in H2O2 scavenging and facilitating the fertilization process
physiological function
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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
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the enzyme is the ovothiol biosynthetic enzyme, ovothiols are histidine-derived thiols
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physiological function
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ovothiol is proposed to be involved in H2O2 scavenging and facilitating the fertilization process
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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
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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
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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
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homologue OvoA_2 is a monofunctional sulfoxide synthase without a C-terminal methyltransferase
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additional information
Moorena producens PAL-8-15-08-1
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an OvoA-like protein, full-length OvoA homologue, OvoA_1, with a C-terminal methyltransferase, most OvoAs contain a C-terminal methyltransferase
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additional information
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the enzyme requires coordination of iron(II) to an unusual iron-binding motif
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