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Literature summary for 1.14.99.52 extracted from

  • Song, H.; Her, A.S.; Raso, F.; Zhen, Z.; Huo, Y.; Liu, P.
    Cysteine oxidation reactions catalyzed by a mononuclear non-heme iron enzyme (OvoA) in ovothiol biosynthesis (2014), Org. Lett., 16, 2122-2125.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.99.52

Application

Application Comment Organism
synthesis potential application of the oxidative coupling between hercynine and cysteine for industrial ergothioneine production Erwinia tasmaniensis

Cloned(Commentary)

Cloned (Comment) Organism
gene ovoA, the mutant enzyme loses the cysteine dioxygenase activity but also stops catalyzing the formation of oxidative coupling product Erwinia tasmaniensis

Protein Variants

Protein Variants Comment Organism
E176H site-directed mutagenesis Erwinia tasmaniensis

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ a mononuclear non-heme iron enzyme, dependent on, ligand with 2-His-1-carboxylate facial triad Erwinia tasmaniensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
-
 ?

Organism

Organism UniProt Comment Textmining
Erwinia tasmaniensis B2VFD8 gene ovoA
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Erwinia tasmaniensis DSM 17950 B2VFD8 gene ovoA
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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-cysteine + O2 oxidation of cysteine to cysteine sulfinic acid in presence of hercynine or L-histidine Erwinia tasmaniensis cysteine sulfinic acid + H2O
-
 ?
L-cysteine + O2 oxidation of cysteine to cysteine sulfinic acid in presence of hercynine or L-histidine Erwinia tasmaniensis DSM 17950 cysteine sulfinic acid + H2O
-
 ?
L-cysteine + O2 oxidation of cysteine to cystine Erwinia tasmaniensis L-cystine + H2O
-
 ?
L-cysteine + O2 oxidation of cysteine to cystine Erwinia tasmaniensis DSM 17950 L-cystine + 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 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 Erwinia tasmaniensis ?
-
 ?
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 Erwinia tasmaniensis DSM 17950 ?
-
 ?

Synonyms

Synonyms Comment Organism
5-histidylcysteine sulfoxide synthase
-
 Erwinia tasmaniensis
OvoA
-
 Erwinia tasmaniensis

General Information

General Information Comment Organism
evolution enzyme OvoA belongs to the 2-His-1-carboxylate catalytic triad type of mononuclear non-heme iron enzymes Erwinia tasmaniensis
malfunction mutation of the 2-His-1-carboxylate catalytic triad of the enzyme disrupts the cysteine dioxygenase activity Erwinia tasmaniensis
metabolism OvoAis required in ovothiol biosynthesis catalyzing the oxidative coupling between histidine and cysteine Erwinia tasmaniensis