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Literature summary for 1.8.3.7 extracted from

  • Knop, M.; Lemnaru, R.; Seebeck, F.P.
    Mutation of conserved residues increases in vitro activity of the formylglycine-generating enzyme (2017), ChemBioChem, 18, 1755-1761 .
    View publication on PubMed
Search for more literature for 1.8.3.7

Protein Variants

Protein Variants Comment Organism
C187A the mutation leads to an increase of enzyme activity Thermomonospora curvata
C187A/C231A/C284S/C298A the mutations lead to an increase of enzyme activity Thermomonospora curvata
C187A/C231A/Y273F/C284S/C298A the mutations lead to an increase of enzyme activity Thermomonospora curvata
C187A/C284S/C298A the mutations lead to an increase of enzyme activity Thermomonospora curvata
C298A the in vitro activity is not affected by the mutation Thermomonospora curvata
Y273F the mutation leads to an increase of enzyme activity Thermomonospora curvata

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.1
-
 Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 mutant C187A/C231A/Y273F/C284S/C298A, at pH 8.0 and 25°C Thermomonospora curvata
0.21
-
 Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 mutant C187A/C231A/C284S/C298A, at pH 8.0 and 25°C Thermomonospora curvata
0.28
-
 Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 mutant C187A/C284S/C298A, at pH 8.0 and 25°C Thermomonospora curvata
0.5
-
 Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 mutant Y273F, at pH 8.0 and 25°C Thermomonospora curvata
0.55
-
 Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 wild type enzyme, at pH 8.0 and 25°C Thermomonospora curvata

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ 0.002 mM used in assay conditions Thermomonospora curvata

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
a [sulfatase]-L-cysteine + O2 + a thiol Thermomonospora curvata
-
 a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Thermomonospora curvata
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
a [sulfatase]-L-cysteine + O2 + a thiol
-
 Thermomonospora curvata a [sulfatase]-3-oxo-L-alanine + hydrogen sulfide + a disulfide + H2O
-
 ?
Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 + O2 + hydrogen sulfide + oxidized dithiothreitol
-
 Thermomonospora curvata ?
-
 ?

Synonyms

Synonyms Comment Organism
FGE
-
 Thermomonospora curvata

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.027
-
 Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 wild type enzyme, at pH 8.0 and 25°C Thermomonospora curvata
0.065
-
 Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 mutant C187A/C284S/C298A, at pH 8.0 and 25°C Thermomonospora curvata
0.07
-
 Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 mutant C187A/C231A/C284S/C298A, at pH 8.0 and 25°C Thermomonospora curvata
0.17
-
 Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 mutant Y273F, at pH 8.0 and 25°C Thermomonospora curvata
0.18
-
 Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 mutant C187A/C231A/Y273F/C284S/C298A, at pH 8.0 and 25°C Thermomonospora curvata

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.0483
-
 Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 wild type enzyme, at pH 8.0 and 25°C Thermomonospora curvata
0.233
-
 Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 mutant C187A/C284S/C298A, at pH 8.0 and 25°C Thermomonospora curvata
0.316
-
 Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 mutant Y273F, at pH 8.0 and 25°C Thermomonospora curvata
0.333
-
 Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 mutant C187A/C231A/C284S/C298A, at pH 8.0 and 25°C Thermomonospora curvata
1.833
-
 Abz-SAL-3-oxo-L-Ala-SPTRA-NH2 mutant C187A/C231A/Y273F/C284S/C298A, at pH 8.0 and 25°C Thermomonospora curvata