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Literature summary for 5.4.99.63 extracted from

  • Erb, T.J.; Retey, J.; Fuchs, G.; Alber, B.E.
    Ethylmalonyl-CoA mutase from Rhodobacter sphaeroides defines a new subclade of coenzyme B12-dependent acyl-CoA mutases (2008), J. Biol. Chem., 283, 32283-32293.
    View publication on PubMed
Search for more literature for 5.4.99.63

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Cereibacter sphaeroides

Crystallization (Commentary)

Crystallization (Comment) Organism
computational modeling using the methylmalonyl-CoA mutase substrate complex from P. freudenreichii subsp. shermanii, Protein Data Bank code 4REQ as template Cereibacter sphaeroides

Protein Variants

Protein Variants Comment Organism
additional information gene insertion mutant is unable to use acetate or acetoacetate as the sole carbon source. Growth on propionate/HCO3-, which requires methylmalonate-CoA mutase, is not affected. Mutant cells do not display ethylmalonyl-CoA converting activity but convert methylmalonyl-CoA to succinyl-CoA Cereibacter sphaeroides

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.06
-
 (2R)-ethylmalonyl-CoA pH 7.8, 30°C Cereibacter sphaeroides

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
74000
-
 2 * 75000, SDS-PAGE, 2 * 74000, calculated Cereibacter sphaeroides
75000
-
 2 * 75000, SDS-PAGE, 2 * 74000, calculated Cereibacter sphaeroides
153000
-
 gel filtration Cereibacter sphaeroides

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Cereibacter sphaeroides enzyme catalyzes the transformation of ethylmalonyl-CoA to methylsuccinyl-CoA in combination with ethylmalonyl-CoA racemase in a ethylmalonyl-CoA dependent acyl-CoA pathway for acetate assimilation ?
-
 ?

Organism

Organism UniProt Comment Textmining
Cereibacter sphaeroides Q3IZ90
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme. Purified recombinant Ecm is unable to form methylsuccinyl-CoA from ethylmalonyl-CoA when ethylmalonyl-CoA is produced by reductive carboxylation of crotonyl-CoA carboxylase/reductase. Addition of cell extract of the gene insertion mutant ecm::kan to the enzyme assay restores ethylmalonyl-CoA mutase activity Cereibacter sphaeroides

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.05
-
 pH 7.8, 30°C Cereibacter sphaeroides

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2R)-ethylmalonyl-CoA purified recombinant Ecm is unable to form methylsuccinyl-CoA from ethylmalonyl-CoA when ethylmalonyl-CoA is produced by reductive carboxylation of crotonyl-CoA carboxylase/reductase. Addition of cell extract of the gene insertion mutant ecm::kan to the enzyme assay restores ethylmalonyl-CoA mutase activity due to presence of ethylmalonyl-CoA epimerase Cereibacter sphaeroides (2S)-methylsuccinyl-CoA
-
 ?
(R)-2-methylmalonyl-CoA 0.2% of the activity with (2R)-ethylmalonyl-CoA Cereibacter sphaeroides succinyl-CoA
-
 ?
additional information enzyme catalyzes the transformation of ethylmalonyl-CoA to methylsuccinyl-CoA in combination with ethylmalonyl-CoA racemase in a ethylmalonyl-CoA dependent acyl-CoA pathway for acetate assimilation Cereibacter sphaeroides ?
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 75000, SDS-PAGE, 2 * 74000, calculated Cereibacter sphaeroides

Synonyms

Synonyms Comment Organism
Ecm
-
 Cereibacter sphaeroides

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5 8 broad Cereibacter sphaeroides

Cofactor

Cofactor Comment Organism Structure
vitamin B12 Km value 0.002 mM Cereibacter sphaeroides