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Literature summary for 4.1.3.25 extracted from

  • Zarzycki, J.; Kerfeld, C.A.
    The crystal structures of the tri-functional Chloroflexus aurantiacus and bi-functional Rhodobacter sphaeroides malyl-CoA lyases and comparison with CitE-like superfamily enzymes and malate synthases (2013), BMC Struct. Biol., 13, 28.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
phylogenetic analysis, recombinant expression in Escherichia coli Chloroflexus aurantiacus

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant enzyme, alone or in complex with substrate propionyl-CoA, inhibitor oxalate, and magnesium ions, pH 5.5, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement modeling Chloroflexus aurantiacus

Inhibitors

Inhibitors Comment Organism Structure
oxalate
-
Chloroflexus aurantiacus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, binding structure, coordination by Glu157 and Asp184, overview Chloroflexus aurantiacus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38400
-
6 * 38400, about, sequence calculation, dimer of trimers, elaborations on the canonical beta8/alpha8 TIM barrel fold and form hexameric assemblies. The trimeric assembly itself is a prerequisite for the catalytic activity Chloroflexus aurantiacus
228000
-
recombinant enzyme, gel filtration Chloroflexus aurantiacus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-citramalyl-CoA Chloroflexus aurantiacus
-
acetyl-CoA + pyruvate
-
r
additional information Chloroflexus aurantiacus the enzyme also performs reactions of EC 4.1.3.24, catalyzing reversible cleavage of (S)-malyl-CoA to acetyl-CoA and glyoxylate, or reversible synthesis of (2R,3S)-2-methylmalyl-CoA from propanoyl-CoA and glyoxylate. Malyl-CoA lyase is a promiscuous carbon-carbon bond lyase that catalyzes the reversible cleavage of structurally related CoA thioesters ?
-
?

Organism

Organism UniProt Comment Textmining
Chloroflexus aurantiacus S5N020
-
-
Chloroflexus aurantiacus OK-70-fl / DSM 636 S5N020
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli Chloroflexus aurantiacus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-citramalyl-CoA
-
Chloroflexus aurantiacus acetyl-CoA + pyruvate
-
r
(S)-citramalyl-CoA the cleavage direction is preferred Chloroflexus aurantiacus acetyl-CoA + pyruvate
-
r
additional information the enzyme also performs reactions of EC 4.1.3.24, catalyzing reversible cleavage of (S)-malyl-CoA to acetyl-CoA and glyoxylate, or reversible synthesis of (2R,3S)-2-methylmalyl-CoA from propanoyl-CoA and glyoxylate. Malyl-CoA lyase is a promiscuous carbon-carbon bond lyase that catalyzes the reversible cleavage of structurally related CoA thioesters Chloroflexus aurantiacus ?
-
?
additional information the enzyme also performs reactions of EC 4.1.3.24, catalyzing reversible cleavage of (S)-malyl-CoA to acetyl-CoA and glyoxylate, or reversible synthesis of (2R,3S)-2-methylmalyl-CoA from propanoyl-CoA and glyoxylate Chloroflexus aurantiacus ?
-
?

Subunits

Subunits Comment Organism
hexamer 6 * 38400, about, sequence calculation, dimer of trimers, elaborations on the canonical beta8/alpha8 TIM barrel fold and form hexameric assemblies. The trimeric assembly itself is a prerequisite for the catalytic activity Chloroflexus aurantiacus

Synonyms

Synonyms Comment Organism
(3S)-3-carboxy-3-hydroxypropanoyl-CoA glyoxylate-lyase UniProt Chloroflexus aurantiacus
(3S)-citramalyl-CoA pyruvate-lyase UniProt Chloroflexus aurantiacus
(S)-citramalyl-CoA lyase UniProt Chloroflexus aurantiacus
malyl-CoA/beta-methylmalyl-CoA/citramalyl-CoA lyase UniProt Chloroflexus aurantiacus
MCL
-
Chloroflexus aurantiacus
MCLC
-
Chloroflexus aurantiacus

General Information

General Information Comment Organism
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) Chloroflexus aurantiacus
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 Chloroflexus aurantiacus
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 Chloroflexus aurantiacus
physiological function the enzyme plays a crucial, multifunctional role in the 3-hydroxypropionate bi-cycle for autotrophic CO2 fixation in Chloroflexus aurantiacus Chloroflexus aurantiacus