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Literature summary extracted from

  • Miarzlou, D.A.; Leisinger, F.; Joss, D.; Haeussinger, D.; Seebeck, F.P.
    Structure of formylglycine-generating enzyme in complex with copper and a substrate reveals an acidic pocket for binding and activation of molecular oxygen (2019), Chem. Sci., 10, 7049-7058 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.3.7 expression in Escherichia coli Thermomonospora curvata

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.8.3.7 1.04 A structure of the enzyme in complex with copper and a cysteine-containing peptide substrate (Abz-ATTPLCGPSRASILSGR) Thermomonospora curvata

Protein Variants

EC Number Protein Variants Comment Organism
1.8.3.7 S266A kcat/Km of the mutant enzyme is fold lower than the wild-type value Thermomonospora curvata
1.8.3.7 W228F kcat/Km of the mutant enzyme is fold lower than the wild-type value Thermomonospora curvata

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.3.7 0.39
-
 Abz-ATTPLCGPSRASILSGR pH 8.0, 25°C, mutant enzyme W228F Thermomonospora curvata
1.8.3.7 0.52
-
 Abz-ATTPLCGPSRASILSGR pH 8.0, 25°C, mutant enzyme S266A Thermomonospora curvata
1.8.3.7 0.53
-
 Abz-ATTPLCGPSRASILSGR pH 8.0, 25°C, wild-type enzyme Thermomonospora curvata

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.8.3.7 Cu(I) the enzyme (FGE) mediates O2-activation and hydrogen-atom abstraction in an active site that contains Cu(I) coordinated to two cysteine residues. The 1.04 A crystal structure of the enzyme in complex with copper and a cysteine-containing peptide substrate unveils a network of four crystallographic waters and two active site residues that form a highly acidic O2-binding pocket juxtaposed to the trigonal planar tris-cysteine coordinated Cu(I) center Thermomonospora curvata

Organism

EC Number Organism UniProt Comment Textmining
1.8.3.7 Thermomonospora curvata D1ADF2
-
-
1.8.3.7 Thermomonospora curvata ATCC 19995 D1ADF2
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.3.7
-
 Thermomonospora curvata

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.3.7 Abz-ATTPLCGPSRASILSGR + O2 + reduced dithiothreitol
-
 Thermomonospora curvata ? + hydrogen sulfide + oxidized dithiothreitol + H2O
-
 ?
1.8.3.7 Abz-ATTPLCGPSRASILSGR + O2 + reduced dithiothreitol
-
 Thermomonospora curvata ATCC 19995 ? + hydrogen sulfide + oxidized dithiothreitol + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.8.3.7 FGE
-
 Thermomonospora curvata
1.8.3.7 formylglycine generating enzyme
-
 Thermomonospora curvata

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.8.3.7 0.00012
-
 Abz-ATTPLCGPSRASILSGR pH 8.0, 25°C, mutant enzyme W228F Thermomonospora curvata
1.8.3.7 0.00042
-
 Abz-ATTPLCGPSRASILSGR pH 8.0, 25°C, mutant enzyme S266A Thermomonospora curvata
1.8.3.7 0.0233
-
 Abz-ATTPLCGPSRASILSGR pH 8.0, 25°C, wild-type enzyme Thermomonospora curvata

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.8.3.7 0.000317
-
 Abz-ATTPLCGPSRASILSGR pH 8.0, 25°C, mutant enzyme W228F Thermomonospora curvata
1.8.3.7 0.00082
-
 Abz-ATTPLCGPSRASILSGR pH 8.0, 25°C, mutant enzyme S266A Thermomonospora curvata
1.8.3.7 0.045
-
 Abz-ATTPLCGPSRASILSGR pH 8.0, 25°C, wild-type enzyme Thermomonospora curvata