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Literature summary for 1.14.99.50 extracted from

  • Goncharenko, K.V.; Seebeck, F.P.
    Conversion of a non-heme iron-dependent sulfoxide synthase into a thiol dioxygenase by a single point mutation (2016), Chem. Commun. (Camb.), 52, 1945-1948 .
    View publication on PubMed
Search for more literature for 1.14.99.50

Protein Variants

Protein Variants Comment Organism
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 Mycolicibacterium thermoresistibile

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-­Menten kinetics Mycolicibacterium thermoresistibile
0.012
-
 hercynine pH 8.0, 26°C, recombinant enzyme mutant Y377F Mycolicibacterium thermoresistibile
0.022
-
 hercynine pH 6.0, 26°C, recombinant enzyme mutant Y377F Mycolicibacterium thermoresistibile

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ the enzyme is a non-heme iron-dependent sulfoxide synthase Mycolicibacterium thermoresistibile

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Mycolicibacterium thermoresistibile G7CFI3
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hercynine + gamma-L-glutamyl-L-cysteine + O2
-
 Mycolicibacterium thermoresistibile gamma-L-glutamyl-S-(hercyn-2-yl)-L-cysteine S-oxide + H2O
-
 ?
additional information product formation is monitored by cation exchange HPLC using 20 mM phosphoric acid at pH 2 as a mobile phase, and EgtB substrates and products are quantified by 1H NMR, overview Mycolicibacterium thermoresistibile ?
-
 ?

Subunits

Subunits Comment Organism
? x * 31600, about, wild-type and mutant enzymes, mass spectrometry Mycolicibacterium thermoresistibile

Synonyms

Synonyms Comment Organism
EgtB
-
 Mycolicibacterium thermoresistibile

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.85
-
 hercynine pH 8.0, 26°C, recombinant enzyme mutant Y377F Mycolicibacterium thermoresistibile
1.2
-
 hercynine pH 6.0, 26°C, recombinant enzyme mutant Y377F Mycolicibacterium thermoresistibile

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 8 assay at, pH 8.0 results in higher catalytic efficiency Mycolicibacterium thermoresistibile

General Information

General Information Comment Organism
malfunction a single point mutation Y377F converts this enzyme into a gamma-glutamyl cysteine dioxygenase with an efficiency that rivals naturally evolved thiol dioxygenases Mycolicibacterium thermoresistibile
physiological function EgtB from Mycobacterium thermoresistibile catalyzes O2-dependent sulfur-carbon bond formation between the side chains of Nalpha-trimethyl histidine and gamma-glutamyl cysteine as a central step in ergothioneine biosynthesis Mycolicibacterium thermoresistibile

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
57
-
 hercynine pH 6.0, 26°C, recombinant enzyme mutant Y377F Mycolicibacterium thermoresistibile
74
-
 hercynine pH 8.0, 26°C, recombinant enzyme mutant Y377F Mycolicibacterium thermoresistibile