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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.1.99.1 expression in Eschserichia coli Cereibacter sphaeroides
5.4.99.63 expression in Escherichia coli Cereibacter sphaeroides

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.4.99.63 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

EC Number Protein Variants Comment Organism
5.4.99.63 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

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.1.99.1 EDTA 2 mM, complete loss of activity Cereibacter sphaeroides

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.1.99.1 0.04
-
 (2S)-ethylmalonyl-CoA
-
 Cereibacter sphaeroides
5.1.99.1 0.08
-
 (S)-methylmalonyl-CoA
-
 Cereibacter sphaeroides
5.4.99.63 0.06
-
 (2R)-ethylmalonyl-CoA pH 7.8, 30°C Cereibacter sphaeroides

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.1.99.1 Co2+ 0.4 mM, 4fold increase in activity. Presence of Co2+ restores activity after incubation with EDTA Cereibacter sphaeroides
5.1.99.1 Mn2+ presence of Mn2+ restores activity after incubation with EDTA Cereibacter sphaeroides
5.1.99.1 additional information no activation of enzyme with Mg2+, Ni2+ Cereibacter sphaeroides

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.4.99.63 74000
-
 2 * 75000, SDS-PAGE, 2 * 74000, calculated Cereibacter sphaeroides
5.4.99.63 75000
-
 2 * 75000, SDS-PAGE, 2 * 74000, calculated Cereibacter sphaeroides
5.4.99.63 153000
-
 gel filtration Cereibacter sphaeroides

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.1.99.1 additional information Cereibacter sphaeroides enzyme catalyzes the transformation of ethylmalonyl-CoA to methylsuccinyl-CoA in combination with ethylmalonyl-CoA mutase, in a ethylmalonyl-CoA dependent acyl-CoA pathway for acetate assimilation ?
-
 ?
5.4.99.63 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

EC Number Organism UniProt Comment Textmining
5.1.99.1 Cereibacter sphaeroides Q3IZP4 promiscuous ethylmalonyl-CoA/methylmalonyl-CoA epimerase
-
5.4.99.63 Cereibacter sphaeroides Q3IZ90
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.99.1 recombinant enzyme Cereibacter sphaeroides
5.4.99.63 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]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.4.99.63 0.05
-
 pH 7.8, 30°C Cereibacter sphaeroides

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.99.1 (2S)-ethylmalonyl-CoA
-
 Cereibacter sphaeroides (2R)-ethylmalonyl-CoA
-
 ?
5.1.99.1 (S)-methylmalonyl-CoA
-
 Cereibacter sphaeroides (R)-methylmalonyl-CoA
-
 ?
5.1.99.1 additional information enzyme catalyzes the transformation of ethylmalonyl-CoA to methylsuccinyl-CoA in combination with ethylmalonyl-CoA mutase, in a ethylmalonyl-CoA dependent acyl-CoA pathway for acetate assimilation Cereibacter sphaeroides ?
-
 ?
5.4.99.63 (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
-
 ?
5.4.99.63 (R)-2-methylmalonyl-CoA 0.2% of the activity with (2R)-ethylmalonyl-CoA Cereibacter sphaeroides succinyl-CoA
-
 ?
5.4.99.63 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

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

Synonyms

EC Number Synonyms Comment Organism
5.4.99.63 Ecm
-
 Cereibacter sphaeroides

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.4.99.63 6.5 8 broad Cereibacter sphaeroides

Cofactor

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