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Literature summary for 4.2.1.113 extracted from

  • Weische, A.; Garvert, W.; Leistner, E.
    Biosynthesis of o-succinylbenzoic acid. II.: Properties of o-succinylbenzoic acid synthase, an enzyme involved in vitamin K2 biosynthesis (1987), Arch. Biochem. Biophys., 256, 223-231.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
EDTA loses all activity during treatment with EDTA, activity is most efficiently restored by Mn2+ Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ restores activity of enzyme inactivated by EDTA Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
66500
-
x * 66500, SDS-PAGE Escherichia coli
195500
-
gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli AN 154
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Escherichia coli

Subunits

Subunits Comment Organism
? x * 66500, SDS-PAGE Escherichia coli

Synonyms

Synonyms Comment Organism
o-succinylbenzoic acid synthase
-
Escherichia coli
OSB synthase
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
Escherichia coli

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
37 60 about 30% of maximal activity at 37°C and at 60°C Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.2
-
-
Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
7.5 9 pH 7.5: about 60% of maximal activity, pH 9.0: about 60% of maximal activity Escherichia coli

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate tightly bound to the enzyme Escherichia coli