Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.4.99.2 extracted from

  • Padovani, D.; Banerjee, R.
    Assembly and protection of the radical enzyme, methylmalonyl-CoA mutase, by its chaperone (2006), Biochemistry, 45, 9300-9306.
    View publication on PubMed
Search for more literature for 5.4.99.2

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.086
-
 (R)-2-methylmalonyl-CoA 37°C Methylorubrum extorquens
0.152
-
 (R)-2-methylmalonyl-CoA presence of P-loop GTPase MeaB and GDP, 37°C Methylorubrum extorquens

Organism

Organism UniProt Comment Textmining
Methylorubrum extorquens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-2-methylmalonyl-CoA
-
 Methylorubrum extorquens succinyl-CoA
-
 ?
additional information P-loop GTPase MeaB plays an auxiliary role in catalytic reaction. MeaB increases affinity of the mutase for cofactor 5’-deoxyadenosylcobalamin twofold Methylorubrum extorquens ?
-
 ?

Subunits

Subunits Comment Organism
More P-loop GTPase MeaB functions in GTP-dependent assembly of holomethyl-malonyl-CoA mutase and subsequent protection of radical intermediates during catalysis Methylorubrum extorquens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
132
-
 (R)-2-methylmalonyl-CoA 37°C Methylorubrum extorquens
237
-
 (R)-2-methylmalonyl-CoA presence of P-loop GTPase MeaB and GDP, 37°C Methylorubrum extorquens
255
-
 (R)-2-methylmalonyl-CoA presence of P-loop GTPase MeaB, 37°C Methylorubrum extorquens

Cofactor

Cofactor Comment Organism Structure
5'-deoxyadenosylcobalamin P-loop GTPase MeaB increases affinity of the mutase for cofactor twofold, in presence of MeaB and GDP, affinity decreases fivifold Methylorubrum extorquens