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Literature summary for 1.14.99.52 extracted from

  • Braunshausen, A.; Seebeck, F.P.
    Identification and characterization of the first ovothiol biosynthetic enzyme (2011), J. Am. Chem. Soc., 133, 1757-1759.
    View publication on PubMed
Search for more literature for 1.14.99.52

Cloned(Commentary)

Cloned (Comment) Organism
gene ovoA, recombinant expression of His-tagged enzyme in Escherichia coli Trypanosoma cruzi
gene ovoA, recombinant expression of His-tagged enzyme in Escherichia coli Erwinia tasmaniensis

Protein Variants

Protein Variants Comment Organism
E176A site-directed mutagenesis, the mutant shows reduced enzyme activity by at least 100fold compared to the wild-type enzyme Erwinia tasmaniensis
H170A site-directed mutagenesis, the mutant shows reduced enzyme activity by at least 100fold compared to the wild-type enzyme Erwinia tasmaniensis
H174A site-directed mutagenesis, the mutant shows reduced enzyme activity by at least 100fold compared to the wild-type enzyme Erwinia tasmaniensis

Metals/Ions

Metals/Ions Comment Organism Structure
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 Trypanosoma cruzi
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 Erwinia tasmaniensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-histidine + L-cysteine + O2 Trypanosoma cruzi
-
 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 Erwinia tasmaniensis DSM 17950
-
 S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
 ?

Organism

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

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography Trypanosoma cruzi
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography Erwinia tasmaniensis

Reaction

Reaction Comment Organism Reaction ID
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 Erwinia tasmaniensis
a
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 Trypanosoma cruzi
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-histidine + L-cysteine + O2
-
 Trypanosoma cruzi 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
-
 Erwinia tasmaniensis DSM 17950 S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
-
 ?

Synonyms

Synonyms Comment Organism
5-histidylcysteine sulfoxide synthase
-
 Trypanosoma cruzi
5-histidylcysteine sulfoxide synthase
-
 Erwinia tasmaniensis
OvoA
-
 Trypanosoma cruzi
OvoA
-
 Erwinia tasmaniensis
OvoAe
-
 Erwinia tasmaniensis
OvoAt
-
 Trypanosoma cruzi

General Information

General Information Comment Organism
metabolism the enzyme is involved in the ovothiol biosynthesis Trypanosoma cruzi
metabolism the enzyme is involved in the ovothiol biosynthesis Erwinia tasmaniensis
additional information the enzyme requires coordination of iron(II) to an unusual iron-binding motif Trypanosoma cruzi
additional information the enzyme requires coordination of iron(II) to an unusual iron-binding motif Erwinia tasmaniensis
physiological function the enzyme is the ovothiol biosynthetic enzyme, ovothiols are histidine-derived thiols Trypanosoma cruzi
physiological function the enzyme is the ovothiol biosynthetic enzyme, ovothiols are histidine-derived thiols Erwinia tasmaniensis