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

BRENDA support

Literature summary for 5.4.99.2 extracted from

  • Nakao, M.; Hironaka, S.; Harada, N.; Adachi, T.; Bito, T.; Yabuta, Y.; Watanabe, F.; Miura, T.; Yamaji, R.; Inui, H.; Nakano, Y.
    Cobalamin deficiency results in an abnormal increase in l-methylmalonyl-co-enzyme-A mutase expression in rat liver and COS-7 cells (2009), Br. J. Nutr., 101, 492-498.
    View publication on PubMed
Search for more literature for 5.4.99.2

Activating Compound

Activating Compound Comment Organism Structure
hydroxocobalamin supplementation of hydroxocobalamin results in a marked increase in the holo-MCM activity in a dose-dependent manner, although the holo-MCM activity does not exceed 30% of the total-MCM activity even if hydroxocobalamin is supplemented at 10 mM Rattus norvegicus

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 (DE3) cells and COS-7 cells Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA agarose resin chromatography Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-2-methylmalonyl-CoA
-
 Rattus norvegicus succinyl-CoA
-
 ?

Synonyms

Synonyms Comment Organism
L-methylmalonyl-co-enzyme-A mutase
-
 Rattus norvegicus
L-methylmalonyl-CoA mutase
-
 Rattus norvegicus
MCM
-
 Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
adenosylcobalamin dependent on adenosylcobalamin as prosthetic group, under cobalamin-deficient conditions, (R)-2-methylmalonyl-CoA and its precursor, propionyl-CoA, increase as a result of a decrease in the catalytic activity of MCM due to deficiency of adenosylcobalamin Rattus norvegicus