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Literature summary for 1.14.99.52 extracted from

  • Peck, S.C.; van der Donk, W.A.
    Go it alone four-electron oxidations by mononuclear non-heme iron enzymes (2017), J. Biol. Inorg. Chem., 22, 381-394 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.99.52

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ non-heme iron, required for catalysis,residues in the HX3HXE motif might be involved in iron binding 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
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 S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
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 ?

Organism

Organism UniProt Comment Textmining
Erwinia tasmaniensis
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-histidine + L-cysteine + O2
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 Erwinia tasmaniensis S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
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 ?
L-histidine + L-cysteine + O2 OvoA modifies the C5 position of the imidazole ring of L-His, site selectivity of the transformation Erwinia tasmaniensis S-(L-histidin-5-yl)-L-cysteine S-oxide + H2O
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 ?
additional information OvoA incubated with hercynine (the normal substrate for EgtB, EC 1.14.99.50) and cysteine produces primarily cysteine sulfinic acid, the product of cysteine dioxygenase-type chemistry, cf. EC 1.13.11.20 Erwinia tasmaniensis ?
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 ?

Synonyms

Synonyms Comment Organism
OvoA
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 Erwinia tasmaniensis
sulfoxide synthase
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 Erwinia tasmaniensis

General Information

General Information Comment Organism
malfunction mutation of any of the residues in the HX3HXE motif in OvoA results in an over 100fold attenuation of activity Erwinia tasmaniensis
additional information residues in the HX3HXE motif are catalytically important (i.e., likely bind iron). Structure homology modeling, overview Erwinia tasmaniensis