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Literature summary for 1.14.99.52 extracted from

  • Song, H.; Leninger, M.; Lee, N.; Liu, P.
    Regioselectivity of the oxidative C-S bond formation in ergothioneine and ovothiol biosyntheses (2013), Org. Lett., 15, 4854-4857.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.99.52

Cloned(Commentary)

Cloned (Comment) Organism
recombinant overexpression of Strep-tagged enzyme in Escherichia coli Erwinia tasmaniensis

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ a mononuclear non-heme iron enzyme, dependent on Erwinia tasmaniensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
hercynine + L-cysteine + O2 Erwinia tasmaniensis
-
 S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
 ?
hercynine + L-cysteine + O2 Erwinia tasmaniensis DSM 17950
-
 S-(hercyn-2-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 Erwinia tasmaniensis DSM 17950
-
 S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
 ?
additional information Erwinia tasmaniensis 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 Erwinia tasmaniensis DSM 17950 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 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Erwinia tasmaniensis B2VFD8 gene ovoA
-
Erwinia tasmaniensis DSM 17950 B2VFD8 gene ovoA
-

Purification (Commentary)

Purification (Comment) Organism
recombinant Strep-tagged enzyme from Escherichia coli by affinity chromatography Erwinia tasmaniensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hercynine + L-cysteine + O2
-
 Erwinia tasmaniensis S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
 ?
hercynine + L-cysteine + O2
-
 Erwinia tasmaniensis DSM 17950 S-(hercyn-2-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
-
 Erwinia tasmaniensis DSM 17950 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 Erwinia tasmaniensis ?
-
 ?
additional information OvoA substrate specificity and substrate binding pocket flexibility, NMR analysis, overview Erwinia tasmaniensis ?
-
 ?
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 Erwinia tasmaniensis DSM 17950 ?
-
 ?
additional information OvoA substrate specificity and substrate binding pocket flexibility, NMR analysis, overview Erwinia tasmaniensis DSM 17950 ?
-
 ?

Synonyms

Synonyms Comment Organism
OvoA
-
 Erwinia tasmaniensis

General Information

General Information Comment Organism
evolution the two known sulfoxide synthases EgtB and OvoA distinguish themselves from each other by their substrate preferences and product C-S bond regioselectivity Erwinia tasmaniensis
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 Erwinia tasmaniensis
physiological function ovothiol is proposed to be involved in H2O2 scavenging and facilitating the fertilization process Erwinia tasmaniensis