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Literature summary for 4.1.3.24 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
Search for more literature for 4.1.3.24

Activating Compound

Activating Compound Comment Organism Structure
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)

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

Inhibitors

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.01
-
 beta-methylmalyl-CoA at 30°C Cereibacter sphaeroides
0.02
-
 (3S)-malyl-CoA at 30°C Cereibacter sphaeroides
0.1
-
 acetyl-CoA at 30°C Cereibacter sphaeroides
0.2
-
 propionyl-CoA at 30°C Cereibacter sphaeroides
3.1
-
 glyoxylate condensation of acetyl-CoA and glyoxylate, at 30°C Cereibacter sphaeroides
4.1
-
 glyoxylate condensation of propionyl-CoA and glyoxylate, at 30°C Cereibacter sphaeroides

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ 73% specific activity at 10 mM Cereibacter sphaeroides
Mn2+ 100% specific activity at 10 mM Cereibacter sphaeroides

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
36800
-
 4 * 36800, by sequence analysis Cereibacter sphaeroides
200000
-
 gel filtration Cereibacter sphaeroides

Organism

Organism UniProt Comment Textmining
Cereibacter sphaeroides Q3J5L6
-
-

Purification (Commentary)

Purification (Comment) Organism
by affinity chromatography Cereibacter sphaeroides

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1
-
 cleavage of (3S)-malyl-CoA Cereibacter sphaeroides
4.5
-
 cleavage of beta-methylmalyl-CoA Cereibacter sphaeroides
14
-
 condensation of acetyl-CoA and glyoxylate Cereibacter sphaeroides
20
-
 condensation of propionyl-CoA and glyoxylate Cereibacter sphaeroides

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(3S)-malyl-CoA
-
 Cereibacter sphaeroides acetyl-CoA + glyoxylate
-
 r
beta-methylmalyl-CoA
-
 Cereibacter sphaeroides glyoxylate + propionyl-CoA
-
 r

Subunits

Subunits Comment Organism
homohexamer 4 * 36800, by sequence analysis Cereibacter sphaeroides

Synonyms

Synonyms Comment Organism
(3S)-malyl-CoA lyase
-
 Cereibacter sphaeroides
(3S)-malyl-coenzyme A lyase
-
 Cereibacter sphaeroides
malyl-CoA lyase
-
 Cereibacter sphaeroides
Mcl1
-
 Cereibacter sphaeroides

Turnover Number [1/s]

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

General Information

General Information Comment Organism
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