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Literature summary for 6.2.1.26 extracted from

  • Siewecke, H.J.; Leistner, E.
    O-Succinylbenzoate:coenzyme A ligase, an enzyme involved in menaquinone (vitamin K2) biosynthesis displays braod specificity (1991), Z. Naturforsch. C, 46, 585-590.
    View publication on PubMed
Search for more literature for 6.2.1.26

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0165
-
 CoA pH 7.2, 30°C Mycolicibacterium phlei
0.1481
-
 o-succinylbenzoate pH 7.2, 30°C Mycolicibacterium phlei
0.4
-
 ATP mutant enzyme H341A Mycolicibacterium phlei

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ 8% of the activation with Mg2+ Mycolicibacterium phlei
Co2+ 63% of the activation with Mg2+ Mycolicibacterium phlei
Cu2+ 7% of the activation with Mg2+ Mycolicibacterium phlei
Mg2+ activation Mycolicibacterium phlei
Mn2+ 36% of the activation with Mg2+ Mycolicibacterium phlei
Ni2+ 46% of the activation with Mg2+ Mycolicibacterium phlei

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
28000
-
 gel filtration Mycolicibacterium phlei

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + 2-succinylbenzoate + CoA Mycolicibacterium phlei o-succinylbenzoyl-CoA is an intermediate in menaquinone (vitamin K2) biosynthesis AMP + diphosphate + 2-succinylbenzoyl-CoA
-
 ?

Organism

Organism UniProt Comment Textmining
Mycolicibacterium phlei
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Mycolicibacterium phlei

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.00084
-
-
 Mycolicibacterium phlei

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 2-succinylbenzoate + CoA
-
 Mycolicibacterium phlei AMP + diphosphate + 2-succinylbenzoyl-CoA incubation of the purified enzyme at different pH values gives a varying ratio of o-succinylbenzoyl-CoA to o-succinylbenzoyl-diCoA. No formation of o-succinylbenzoyl-2-CoA. No formation of ADP ?
ATP + 2-succinylbenzoate + CoA o-succinylbenzoyl-CoA is an intermediate in menaquinone (vitamin K2) biosynthesis Mycolicibacterium phlei AMP + diphosphate + 2-succinylbenzoyl-CoA
-
 ?
ATP + 2-succinylbenzoate + dephospho-CoA 96% of the activity with CoA Mycolicibacterium phlei AMP + 2-succinylbenzoyldephospho-CoA + diphosphate
-
 ?
ATP + benzoylpropionic acid + CoA 21.6% of the activity with o-succinylbenzoate Mycolicibacterium phlei AMP + benzoylpropionyl-CoA + diphosphate
-
 ?
ATP + o-malonylbenzoate + CoA 11.6% of the activity with o-succinylnemzoate Mycolicibacterium phlei AMP + o-malonylbenzoyl-CoA + diphosphate
-
 ?
CTP + o-succinylbenzoate + CoA 13.5% of the activity with ATP Mycolicibacterium phlei CMP + diphosphate + o-succinylbenzoyl-CoA
-
 ?
GTP + o-succinylbenzoate + CoA 13.4% of the activity with ATP Mycolicibacterium phlei GMP + diphosphate + o-succinylbenzoyl-CoA
-
 ?
ITP + o-succinylbenzoate + CoA 10.9% of the activity with ATP Mycolicibacterium phlei IMP + diphosphate + o-succinylbenzoyl-CoA
-
 ?
TTP + o-succinylbenzoate + CoA 12.1% of the activity with ATP Mycolicibacterium phlei TMP + diphosphate + o-succinylbenzoyl-CoA
-
 ?
UTP + o-succinylbenzoate + CoA 12.3% of the activity with ATP Mycolicibacterium phlei UMP + diphosphate + o-succinylbenzoyl-CoA
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
38
-
-
 Mycolicibacterium phlei

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
-
 Mycolicibacterium phlei

pI Value

Organism Comment pI Value Maximum pI Value
Mycolicibacterium phlei isoelectric focusing
-
 4.9