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1.14.99.50: gamma-glutamyl hercynylcysteine S-oxide synthase

This is an abbreviated version!
For detailed information about gamma-glutamyl hercynylcysteine S-oxide synthase, go to the full flat file.

Word Map on EC 1.14.99.50

Reaction

hercynine
+
gamma-L-glutamyl-L-cysteine
 +
O2
=
gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide
 +
H2O

Synonyms

5-histidylcysteine sulfoxide synthase, Cabther_A1318, EgtB, EgtBthermo, hercynine oxygenase, sulfoxide synthase

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.99 Miscellaneous
                1.14.99.50 gamma-glutamyl hercynylcysteine S-oxide synthase

Engineering

Engineering on EC 1.14.99.50 - gamma-glutamyl hercynylcysteine S-oxide synthase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A420Y
position is involved in controlling the reaction selectiviy. Mutant leads to an increased amount of side-reaction (cysteine dioxygenase activity)
D52L
mutation may disrupt the hydrogen bond between Asp52 and glutamyl group of substrate gamma-Glu-Cys, which in turn alters the substrate selectivity
D52L/A420Y
mutation tunes EgtB activity toward Egt1-type, i.e. reaction of EC 1.21.3.10
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
D416N
site-directed mutagenesis, the mutation increases KM for gamma-glutamyl cysteine by 200fold but does not significantly change KM for N-alpha-trimethyl histidine or kcat compared to the wild-type enzyme
Y377F
site-directed mutagenesis, the mutation results in conversion of the non-heme iron-dependent sulfoxide synthase into a thiol dioxygenase, purified enzyme mutant EgtBY377F contains 0.64% equiv. of iron as inferred by a ferrozine-based colorimetric assay, and shows reduced activity compared to the wild-type enzyme