4.1.3.24: malyl-CoA lyase
This is an abbreviated version!
For detailed information about malyl-CoA lyase, go to the full flat file.
Word Map on EC 4.1.3.24
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4.1.3.24
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malate
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methylobacterium
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extorquens
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facultative
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3-hydroxypropionate
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methanol
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carboxylase
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propionyl-coa
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sphaeroides
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chloroflexus
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phosphoenolpyruvate
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rhodobacter
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phototrophic
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aurantiacus
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ethylmalonyl-coa
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hydroxypyruvate
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one-carbon
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thioesters
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acetyl-coenzyme
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ribulose
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succinyl-coa
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lyases
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carbon-carbon
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roseiflexus
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succinate-grown
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multicarbon
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3-hydroxybutyrate
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calvin
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condenses
- 4.1.3.24
- malate
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methylobacterium
- extorquens
-
facultative
- 3-hydroxypropionate
- methanol
- carboxylase
- propionyl-coa
- sphaeroides
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chloroflexus
- phosphoenolpyruvate
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rhodobacter
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phototrophic
- aurantiacus
- ethylmalonyl-coa
- hydroxypyruvate
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one-carbon
- thioesters
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acetyl-coenzyme
- ribulose
- succinyl-coa
- lyases
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carbon-carbon
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roseiflexus
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succinate-grown
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multicarbon
- 3-hydroxybutyrate
-
calvin
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condenses
Reaction
Synonyms
(3S)-malyl-CoA lyase, (3S)-malyl-coenzyme A lyase, L-malyl-CoA lyase/beta-methylmalyl-CoA lyase, L-malyl-CoA/beta-methylmalyl-CoA lyase, L-malyl-coenzyme A/beta-methylmalyl-coenzyme A lyase, lyase, malyl coenzyme A, malyl coenzyme A lyase, malyl-CoA lyase, malyl-CoA/beta-methylmalyl-CoA lyase, malyl-CoA/beta-methylmalyl-CoA/citramalyl-CoA lyase, MCL, Mcl1, MCLC, MCLR
ECTree
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General Information
General Information on EC 4.1.3.24 - malyl-CoA lyase
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evolution
metabolism
physiological function
additional information
the enzyme belongs to the large superfamily of CitE-like enzymes, which includes the beta-subunit of citrate lyase (CitE), malyl-CoA thioesterases and other enzymes of unknown physiological function. The CitE-like enzyme superfamily also bears sequence and structural resemblance to the malate synthases. All of these different enzymes share highly conserved catalytic residues, although they catalyze distinctly different reactions: C-C bond formation and cleavage, thioester hydrolysis, or both (the malate synthases)
evolution
the enzyme belongs to the large superfamily of CitE-like enzymes, which includes the beta-subunit of citrate lyase (CitE), malyl-CoA thioesterases and other enzymes of unknown physiological function. The CitE-like enzyme superfamily also bears sequence and structural resemblance to the malate synthases. All of these different enzymes share highly conserved catalytic residues, although they catalyze distinctly different reactions: C-C bond formation and cleavage, thioester hydrolysis, or both (the malate synthases)
evolution
Chloroflexus aurantiacus OK-70-fl / DSM 636
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the enzyme belongs to the large superfamily of CitE-like enzymes, which includes the beta-subunit of citrate lyase (CitE), malyl-CoA thioesterases and other enzymes of unknown physiological function. The CitE-like enzyme superfamily also bears sequence and structural resemblance to the malate synthases. All of these different enzymes share highly conserved catalytic residues, although they catalyze distinctly different reactions: C-C bond formation and cleavage, thioester hydrolysis, or both (the malate synthases)
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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
metabolism
the enzyme belongs to a group of organisms that lack isocitrate lyase. Therefore, they are unable to use the glyoxylate bypass to assimilate acetyl-CoA or other substrates that enter central carbon metabolism at the level of acetyl-CoA. Instead, they use the ethylmalonyl-CoA pathway for the assimilation of acetyl-CoA with the bifunctional enzyme catalyzing the cleavage of beta-methylmalyl-CoA and the synthesis of malyl-CoA
metabolism
the enzyme catalyzes three different steps in the 3-hydroxypropionate bi-cycle for autotrophic CO2 fixation, the tri-functionality of the MCLC underscores its key role for this pathway
metabolism
Chloroflexus aurantiacus OK-70-fl / DSM 636
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the enzyme catalyzes three different steps in the 3-hydroxypropionate bi-cycle for autotrophic CO2 fixation, the tri-functionality of the MCLC underscores its key role for this pathway
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the enzyme from Rhodobacter sphaeroides is involved in the ethylmalonyl-CoA pathway for acetate assimilation
physiological function
the enzyme plays a crucial, multifunctional role in the 3-hydroxypropionate bi-cycle for autotrophic CO2 fixation in Chloroflexus aurantiacus
physiological function
Chloroflexus aurantiacus OK-70-fl / DSM 636
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the enzyme plays a crucial, multifunctional role in the 3-hydroxypropionate bi-cycle for autotrophic CO2 fixation in Chloroflexus aurantiacus
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upon ligand binding, changes in the C-terminal domains of the enzyme results in closing of the active site, with the C-terminal domain of one monomer forming a lid over and contributing side chains to the active site of the adjacent monomer, overview
additional information
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upon ligand binding, changes in the C-terminal domains of the enzyme results in closing of the active site, with the C-terminal domain of one monomer forming a lid over and contributing side chains to the active site of the adjacent monomer, overview
additional information
upon ligand binding, changes in the C-terminal domains of the enzyme results in closing of the active site, with the C-terminal domain of one monomer forming a lid over and contributing side chains to the active site of the adjacent monomer, overview
additional information
-
upon ligand binding, changes in the C-terminal domains of the enzyme results in closing of the active site, with the C-terminal domain of one monomer forming a lid over and contributing side chains to the active site of the adjacent monomer, overview
additional information
Chloroflexus aurantiacus OK-70-fl / DSM 636
-
upon ligand binding, changes in the C-terminal domains of the enzyme results in closing of the active site, with the C-terminal domain of one monomer forming a lid over and contributing side chains to the active site of the adjacent monomer, overview
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