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Literature summary for 1.14.99.50 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 1.14.99.50

Protein Variants

Protein Variants Comment Organism
Y377F site-directed mutagenesis, the single point mutation in EgtB completely uncouples substrate consumption from sulfoxide synthase activity with the native substrates hercynine and gamma-glutamyl cysteine, with EgtB exclusively oxidizing gamma-glutamyl cysteine to the sulfinic acid. Tyr377 is hydrogen bonded to a water molecule that coordinates to the iron Mycobacterium avium

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ non-heme iron, required for catalysis, the active site iron is coordinated by a 3-His facial triad rather than a 2-His-1-Glu ligand set Mycobacterium avium

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
hercynine + gamma-L-glutamyl-L-cysteine + O2 Mycobacterium avium
-
 gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium avium
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hercynine + gamma-L-glutamyl-L-cysteine + O2
-
 Mycobacterium avium gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
 ?
hercynine + gamma-L-glutamyl-L-cysteine + O2 sulfoxide incorporation at C2 by EgtB Mycobacterium avium gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
 ?
additional information no activity with L-cysteine and L-histdine Mycobacterium avium ?
-
 ?

Synonyms

Synonyms Comment Organism
5-histidylcysteine sulfoxide synthase
-
 Mycobacterium avium
EgtB
-
 Mycobacterium avium

General Information

General Information Comment Organism
evolution EgtB contains a strongly conserved HX3HXE motif, implying that it is a member of the facial triad enzyme family with the Fe(II) site ligated by 2-His-1-Glu Mycobacterium avium