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Literature summary for 1.14.99.52 extracted from

  • Liao, C.; Seebeck, F.P.
    Convergent evolution of ergothioneine biosynthesis in cyanobacteria (2017), ChemBioChem, 18, 2115-2118 .
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ an iron-dependent sulfoxide synthase Microcystis aeruginosa
Fe2+ an iron-dependent sulfoxide synthase Moorena producens
Fe2+ an iron-dependent sulfoxide synthase Erwinia tasmaniensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
hercynine + gamma-L-glutamyl-L-cysteine + O2 Moorena producens
-
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
?
hercynine + gamma-L-glutamyl-L-cysteine + O2 Moorena producens PAL-8-15-08-1
-
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
?
L-histidine + L-cysteine + O2 Moorena producens
-
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
?
L-histidine + L-cysteine + O2 Moorena producens PAL-8-15-08-1
-
S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
?
additional information Moorena producens an OvoA-like protein, full-length OvoA homologue, OvoA_2, is a monofunctional sulfoxide synthase ?
-
?
additional information Microcystis aeruginosa short cyanobacterial OvoA-type enzymes may contribute to ergothioneine (EC 1.14.99.51) instead of ovothiol production ?
-
?
additional information Erwinia tasmaniensis 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 Moorena producens PAL-8-15-08-1 an OvoA-like protein, full-length OvoA homologue, OvoA_2, is a monofunctional sulfoxide synthase ?
-
?

Organism

Organism UniProt Comment Textmining
Erwinia tasmaniensis
-
-
-
Microcystis aeruginosa
-
-
-
Moorena producens A0A1D8U0C7
-
-
Moorena producens A0A1D8U386
-
-
Moorena producens PAL-8-15-08-1 A0A1D8U0C7
-
-
Moorena producens PAL-8-15-08-1 A0A1D8U386
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hercynine + gamma-L-glutamyl-L-cysteine + O2
-
Moorena producens gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
?
hercynine + gamma-L-glutamyl-L-cysteine + O2
-
Moorena producens PAL-8-15-08-1 gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
?
L-histidine + L-cysteine + O2
-
Microcystis aeruginosa S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
?
L-histidine + L-cysteine + O2
-
Moorena producens S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
?
L-histidine + L-cysteine + O2
-
Erwinia tasmaniensis S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
?
L-histidine + L-cysteine + O2
-
Moorena producens PAL-8-15-08-1 S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
?
additional information an OvoA-like protein, full-length OvoA homologue, OvoA_2, is a monofunctional sulfoxide synthase Moorena producens ?
-
?
additional information short cyanobacterial OvoA-type enzymes may contribute to ergothioneine (EC 1.14.99.51) instead of ovothiol production Microcystis aeruginosa ?
-
?
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 Erwinia tasmaniensis ?
-
?
additional information 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 Moorena producens ?
-
?
additional information an OvoA-like protein, full-length OvoA homologue, OvoA_2, is a monofunctional sulfoxide synthase Moorena producens PAL-8-15-08-1 ?
-
?
additional information 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 Moorena producens PAL-8-15-08-1 ?
-
?

Synonyms

Synonyms Comment Organism
OvoA
-
Moorena producens
OvoA-like protein
-
Microcystis aeruginosa
OvoA-like protein
-
Moorena producens
OvoAErwin
-
Erwinia tasmaniensis
OvoA_1
-
Moorena producens
OvoA_2
-
Moorena producens
short OvoA homologue
-
Microcystis aeruginosa

General Information

General Information Comment Organism
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 Microcystis aeruginosa
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 Moorena producens
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 Erwinia tasmaniensis
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 Microcystis aeruginosa
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 Moorena producens
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 Erwinia tasmaniensis
additional information an OvoA-like protein, full-length OvoA homologue, OvoA_1, with a C-terminal methyltransferase, most OvoAs contain a C-terminal methyltransferase Moorena producens
additional information homologue OvoA_2 is a monofunctional sulfoxide synthase without a C-terminal methyltransferase Moorena producens