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Literature summary extracted from

  • Erb, T.J.; Frerichs-Revermann, L.; Fuchs, G.; Alber, B.E.
    The apparent malate synthase activity of Rhodobacter sphaeroides is due to two paralogous enzymes, (3S)-Malyl-coenzyme A (CoA)/{beta}-methylmalyl-CoA lyase and (3S)-Malyl-CoA thioesterase (2010), J. Bacteriol., 192, 1249-1258.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.1.3.24 acetate growth of the mcl1::kan mutant on acetate is not rescued by the addition of glyoxylate, the mutant growth rates are comparable to those of the wild type on substrates downstream of the proposed metabolic block, i.e., malate and propionate plus bicarbonate Cereibacter sphaeroides

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.2.30 expression in Escherichia coli Cereibacter sphaeroides
4.1.3.24 into pET16b and expressed as an N-terminal deca-His tag fusion protein in Escherichia coli BL21(DE3) cells Cereibacter sphaeroides

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.2.30 EDTA reversible inhibition Cereibacter sphaeroides
4.1.3.24 Ca2+ 14% specific activity at 10 mM Cereibacter sphaeroides
4.1.3.24 Co2+ 13% specific activity at 10 mM Cereibacter sphaeroides
4.1.3.24 EDTA 1% specific activity at 10 mM Cereibacter sphaeroides
4.1.3.24 Ni2+ 6% specific activity at 10 mM Cereibacter sphaeroides
4.1.3.24 succinate activity is downregulated 10fold Cereibacter sphaeroides

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.2.30 0.09
-
(S)-malyl-CoA pH 7.5, 30°C, in the presence of divalent cations (Mg2+ or Mn2+) Cereibacter sphaeroides
4.1.3.24 0.01
-
beta-methylmalyl-CoA at 30°C Cereibacter sphaeroides
4.1.3.24 0.02
-
(3S)-malyl-CoA at 30°C Cereibacter sphaeroides
4.1.3.24 0.1
-
acetyl-CoA at 30°C Cereibacter sphaeroides
4.1.3.24 0.2
-
propionyl-CoA at 30°C Cereibacter sphaeroides
4.1.3.24 3.1
-
glyoxylate condensation of acetyl-CoA and glyoxylate, at 30°C Cereibacter sphaeroides
4.1.3.24 4.1
-
glyoxylate condensation of propionyl-CoA and glyoxylate, at 30°C Cereibacter sphaeroides

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.2.30 Mg2+ 10 mM, stimulated by Mg2+ or Mn2+ Cereibacter sphaeroides
3.1.2.30 Mn2+ 10 mM, stimulated by Mg2+ or Mn2+ Cereibacter sphaeroides
4.1.3.24 Mg2+ 73% specific activity at 10 mM Cereibacter sphaeroides
4.1.3.24 Mn2+ 100% specific activity at 10 mM Cereibacter sphaeroides

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.2.30 33400
-
2 * or 3 * x * 33400, calculated from sequence Cereibacter sphaeroides
3.1.2.30 80000
-
gel filtration Cereibacter sphaeroides
4.1.3.24 36800
-
4 * 36800, by sequence analysis Cereibacter sphaeroides
4.1.3.24 200000
-
gel filtration Cereibacter sphaeroides

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.2.30 (S)-malyl-CoA + H2O Cereibacter sphaeroides the enzyme is involved in the ethylmalonyl-CoA pathway for acetyl-CoA assimilation (S)-malate + CoA
-
?
3.1.2.30 (S)-malyl-CoA + H2O Cereibacter sphaeroides DSM 158 the enzyme is involved in the ethylmalonyl-CoA pathway for acetyl-CoA assimilation (S)-malate + CoA
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.1.2.30 Cereibacter sphaeroides D3JV05
-
-
3.1.2.30 Cereibacter sphaeroides DSM 158 D3JV05
-
-
4.1.3.24 Cereibacter sphaeroides Q3J5L6
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.2.30 recombinant His-tagged proteins Cereibacter sphaeroides
4.1.3.24 by affinity chromatography Cereibacter sphaeroides

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.2.30 200
-
thioester cleavage, pH 7.5, 30°C Cereibacter sphaeroides
4.1.3.24 4.1
-
cleavage of (3S)-malyl-CoA Cereibacter sphaeroides
4.1.3.24 4.5
-
cleavage of beta-methylmalyl-CoA Cereibacter sphaeroides
4.1.3.24 14
-
condensation of acetyl-CoA and glyoxylate Cereibacter sphaeroides
4.1.3.24 20
-
condensation of propionyl-CoA and glyoxylate Cereibacter sphaeroides

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.2.30 (S)-malyl-CoA + H2O the enzyme is involved in the ethylmalonyl-CoA pathway for acetyl-CoA assimilation Cereibacter sphaeroides (S)-malate + CoA
-
?
3.1.2.30 (S)-malyl-CoA + H2O (S)-malyl-CoA i.e. (3S)-3-carboxy-3-hydroxypropanoyl-CoA, the enzyme has no activity with (2R,3S)-2-methylmalyl-CoA (cf. EC 4.1.3.24, malyl-CoA lyase) or other CoA esters Cereibacter sphaeroides (S)-malate + CoA
-
?
3.1.2.30 (S)-malyl-CoA + H2O the enzyme is involved in the ethylmalonyl-CoA pathway for acetyl-CoA assimilation Cereibacter sphaeroides DSM 158 (S)-malate + CoA
-
?
3.1.2.30 (S)-malyl-CoA + H2O (S)-malyl-CoA i.e. (3S)-3-carboxy-3-hydroxypropanoyl-CoA, the enzyme has no activity with (2R,3S)-2-methylmalyl-CoA (cf. EC 4.1.3.24, malyl-CoA lyase) or other CoA esters Cereibacter sphaeroides DSM 158 (S)-malate + CoA
-
?
4.1.3.24 (3S)-malyl-CoA
-
Cereibacter sphaeroides acetyl-CoA + glyoxylate
-
r
4.1.3.24 beta-methylmalyl-CoA
-
Cereibacter sphaeroides glyoxylate + propionyl-CoA
-
r

Subunits

EC Number Subunits Comment Organism
3.1.2.30 ? 2 * or 3 * x * 33400, calculated from sequence Cereibacter sphaeroides
4.1.3.24 homohexamer 4 * 36800, by sequence analysis Cereibacter sphaeroides

Synonyms

EC Number Synonyms Comment Organism
3.1.2.30 Mcl2
-
Cereibacter sphaeroides
4.1.3.24 (3S)-malyl-CoA lyase
-
Cereibacter sphaeroides
4.1.3.24 (3S)-malyl-coenzyme A lyase
-
Cereibacter sphaeroides
4.1.3.24 malyl-CoA lyase
-
Cereibacter sphaeroides
4.1.3.24 Mcl1
-
Cereibacter sphaeroides

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.2.30 30
-
assay at Cereibacter sphaeroides

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.2.30 110
-
(S)-malyl-CoA pH 7.5, 30°C Cereibacter sphaeroides
4.1.3.24 2.5
-
(3S)-malyl-CoA at 30°C Cereibacter sphaeroides
4.1.3.24 2.8
-
beta-methylmalyl-CoA at 30°C Cereibacter sphaeroides
4.1.3.24 8.6
-
acetyl-CoA at 30°C Cereibacter sphaeroides
4.1.3.24 12
-
propionyl-CoA at 30°C Cereibacter sphaeroides

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.2.30 7.5
-
assay at Cereibacter sphaeroides

General Information

EC Number General Information Comment Organism
3.1.2.30 physiological function the enzyme is involved in the ethylmalonyl-CoA pathway for acetyl-CoA assimilation Cereibacter sphaeroides
4.1.3.24 metabolism Mcl1 and Mcl2 together catalyze the apparent malate synthase activity during acetyl-CoA assimilation via the ethylmalonyl-CoA pathway. Mcl1 is a true (3S)-malyl-CoA lyase, catalyzing the Claisen condensation of acetyl-CoA with glyoxylate. Activity of the mcl1::kan mutant is not detected in cell extracts grown on succinate plus acetate. Apparent malate synthase activity is very low in cell extracts of the mcl1::kan and mcl2::kan mutants when grown on acetate or acetate plus succinate Cereibacter sphaeroides

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.1.2.30 1200
-
(S)-malyl-CoA pH 7.5, 30°C Cereibacter sphaeroides