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Information on EC 4.1.3.24 - malyl-CoA lyase
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4.1.3.24 malyl-CoA lyaseIUBMB Comments
The enzymes from Rhodobacter species catalyse a step in the ethylmalonyl-CoA pathway for acetate assimilation [3,5]. The enzyme from halophilic bacteria participate in the methylaspartate cycle and catalyse the reaction in the direction of malyl-CoA formation . The enzyme from the bacterium Chloroflexus aurantiacus, which participates in the 3-hydroxypropanoate cycle for carbon assimilation, also has the activity of EC 4.1.3.25, (3S)-citramalyl-CoA lyase [2,4].
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Word Map
- 4.1.3.24
- malate
-
methylobacterium
- extorquens
-
facultative
- 3-hydroxypropionate
- methanol
- carboxylase
- propionyl-coa
- sphaeroides
-
chloroflexus
- phosphoenolpyruvate
-
rhodobacter
-
phototrophic
- aurantiacus
- ethylmalonyl-coa
- hydroxypyruvate
-
one-carbon
- thioesters
-
acetyl-coenzyme
- ribulose
- succinyl-coa
- lyases
-
carbon-carbon
-
roseiflexus
-
succinate-grown
-
multicarbon
- 3-hydroxybutyrate
-
calvin
-
condenses
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
Synonyms
malyl-coa lyase, l-malyl-coa lyase/beta-methylmalyl-coa lyase, malyl coenzyme a lyase, malyl-coa/beta-methylmalyl-coa lyase, (3s)-malyl-coa lyase, l-malyl-coa/beta-methylmalyl-coa lyase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-malyl-CoA lyase/beta-methylmalyl-CoA lyase
-
the two enzymes are identical and both enzymatic reactions are catalysed by one single bifunctional enzyme
lyase, malyl coenzyme A
-
-
-
-
malyl coenzyme A lyase
-
-
-
-
malyl-CoA/beta-methylmalyl-CoA lyase
malyl-CoA/beta-methylmalyl-CoA/citramalyl-CoA lyase
MCL
MCLC
malyl-CoA/beta-methylmalyl-CoA lyase
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
protein MclA2
-
malyl-CoA/beta-methylmalyl-CoA/citramalyl-CoA lyase
Chloroflexus aurantiacus OK-70-fl / DSM 636
UniProt
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2R,3S)-2-methylmalyl-CoA = propanoyl-CoA + glyoxylate
(2)
-
-
-
(S)-malyl-CoA = acetyl-CoA + glyoxylate
in the reverse direction ordered sequential mechanism with glyoxylate binding prior to acetyl-CoA
-
(S)-malyl-CoA = acetyl-CoA + glyoxylate
(1)
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
of an oxo-acid, C-C bond cleavage
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
(S)-malyl-CoA glyoxylate-lyase (acetyl-CoA-forming)
The enzymes from Rhodobacter species catalyse a step in the ethylmalonyl-CoA pathway for acetate assimilation [3,5]. The enzyme from halophilic bacteria participate in the methylaspartate cycle and catalyse the reaction in the direction of malyl-CoA formation [6]. The enzyme from the bacterium Chloroflexus aurantiacus, which participates in the 3-hydroxypropanoate cycle for carbon assimilation, also has the activity of EC 4.1.3.25, (3S)-citramalyl-CoA lyase [2,4].
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CAS REGISTRY NUMBER
COMMENTARY
37290-67-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
propionyl-CoA + glyoxylate
(2S)-4-(beta-methyl)-malyl-CoA
-
-
-
r
(2R,3S)-2-methylmalyl-CoA
propanoyl-CoA + glyoxylate
the synthesis direction is preferred
-
-
r
(2R,3S)-2-methylmalyl-CoA
propanoyl-CoA + glyoxylate
the synthesis direction is preferred
-
-
r
(2R,3S)-2-methylmalyl-CoA
propanoyl-CoA + glyoxylate
Chloroflexus aurantiacus OK-70-fl / DSM 636
-
-
-
r
(2R,3S)-2-methylmalyl-CoA
propanoyl-CoA + glyoxylate
Chloroflexus aurantiacus OK-70-fl / DSM 636
the synthesis direction is preferred
-
-
r
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
r
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
malyl-CoA
-
r
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
enzyme in 3-hydroxypropionate cycle
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
Chloroflexus aurantiacus OK-70-fl / DSM 636
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
Chloroflexus aurantiacus OK-70-fl / DSM 636
-
enzyme in 3-hydroxypropionate cycle
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
Methylobacterium hypolimneticum
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
Methylobacterium methanolicum
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
r
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
r
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
Pseudomonas methanolica
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
?
(S)-malyl-CoA
acetyl-CoA + glyoxylate
the cleavage direction is preferred
-
-
r
(S)-malyl-CoA
acetyl-CoA + glyoxylate
the cleavage direction is preferred
-
-
r
acetyl-CoA + glyoxylate
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
-
-
-
r
acetyl-CoA + glyoxylate
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
-
-
-
r
beta-methylmalyl-CoA
glyoxylate + propionyl-CoA
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
-
-
-
?
propionyl-CoA + glyoxylate
erythro-beta-methylmalyl-CoA
-
-
-
?
additional information
?
-
malyl-CoA lyase is a promiscuous carbon-carbon bond lyase that catalyzes the reversible cleavage of structurally related CoA thioesters
-
-
?
additional information
?
-
-
malyl-CoA lyase is a promiscuous carbon-carbon bond lyase that catalyzes the reversible cleavage of structurally related CoA thioesters
-
-
?
additional information
?
-
modeling of binding structures of glyoxylate, acetyl-CoA, pyruvate, and Mg2+, overview
-
-
?
additional information
?
-
-
modeling of binding structures of glyoxylate, acetyl-CoA, pyruvate, and Mg2+, overview
-
-
?
additional information
?
-
the enzyme also catalzes the reversible cleavage of (S)-citramalyl-CoA to acetyl-CoA and pyruvate, reaction of EC 4.1.3.25. Malyl-CoA lyase is a promiscuous carbon-carbon bond lyase that catalyzes the reversible cleavage of structurally related CoA thioesters
-
-
?
additional information
?
-
-
the enzyme also catalzes the reversible cleavage of (S)-citramalyl-CoA to acetyl-CoA and pyruvate, reaction of EC 4.1.3.25. Malyl-CoA lyase is a promiscuous carbon-carbon bond lyase that catalyzes the reversible cleavage of structurally related CoA thioesters
-
-
?
additional information
?
-
the enzyme also catalzes the reversible cleavage of (S)-citramalyl-CoA to acetyl-CoA and pyruvate, reaction of EC 4.1.3.25
-
-
?
additional information
?
-
-
the enzyme also catalzes the reversible cleavage of (S)-citramalyl-CoA to acetyl-CoA and pyruvate, reaction of EC 4.1.3.25
-
-
?
additional information
?
-
Chloroflexus aurantiacus OK-70-fl / DSM 636
the enzyme also catalzes the reversible cleavage of (S)-citramalyl-CoA to acetyl-CoA and pyruvate, reaction of EC 4.1.3.25. Malyl-CoA lyase is a promiscuous carbon-carbon bond lyase that catalyzes the reversible cleavage of structurally related CoA thioesters
-
-
?
additional information
?
-
Chloroflexus aurantiacus OK-70-fl / DSM 636
the enzyme also catalzes the reversible cleavage of (S)-citramalyl-CoA to acetyl-CoA and pyruvate, reaction of EC 4.1.3.25
-
-
?
additional information
?
-
-
the role in C1 metabolism, in organisms utilizing the Ser pathway, may be to provide the glyoxylate necessary to sustain operations of this pathway
-
-
?
additional information
?
-
-
the role in C1 metabolism, in organisms utilizing the Ser pathway, may be to provide the glyoxylate necessary to sustain operations of this pathway
-
-
?
additional information
?
-
-
the enzyme may serve as a route to Gly during biosynthesis of purines and proteins
-
-
?
additional information
?
-
-
the role in C1 metabolism, in organisms utilizing the Ser pathway, may be to provide the glyoxylate necessary to sustain operations of this pathway
-
-
?
additional information
?
-
-
the role in C1 metabolism, in organisms utilizing the Ser pathway, may be to provide the glyoxylate necessary to sustain operations of this pathway
-
-
?
additional information
?
-
Pseudomonas methanolica
-
the enzyme may serve as a route to Gly during biosynthesis of purines and proteins
-
-
?
additional information
?
-
-
the specific activity of malyl-CoA lyase is severalfold higher when grown on C1 compounds than when grown on C2, C3 or C4 compounds
-
-
?
additional information
?
-
-
the specific activity of malyl-CoA lyase is severalfold higher when grown on C1 compounds than when grown on C2, C3 or C4 compounds
-
-
?
additional information
?
-
-
the specific activity of malyl-CoA lyase is severalfold higher when grown on C1 compounds than when grown on C2, C3 or C4 compounds
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
propionyl-CoA + glyoxylate
(2S)-4-(beta-methyl)-malyl-CoA
-
-
-
r
(2R,3S)-2-methylmalyl-CoA
propanoyl-CoA + glyoxylate
Chloroflexus aurantiacus OK-70-fl / DSM 636
-
-
-
r
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
-
-
r
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
-
enzyme in 3-hydroxypropionate cycle
-
?
(3S)-3-carboxy-3-hydroxypropanoyl-CoA
acetyl-CoA + glyoxylate
Chloroflexus aurantiacus OK-70-fl / DSM 636
-
enzyme in 3-hydroxypropionate cycle
-
?
additional information
?
-
malyl-CoA lyase is a promiscuous carbon-carbon bond lyase that catalyzes the reversible cleavage of structurally related CoA thioesters
-
-
?
additional information
?
-
-
malyl-CoA lyase is a promiscuous carbon-carbon bond lyase that catalyzes the reversible cleavage of structurally related CoA thioesters
-
-
?
additional information
?
-
the enzyme also catalzes the reversible cleavage of (S)-citramalyl-CoA to acetyl-CoA and pyruvate, reaction of EC 4.1.3.25. Malyl-CoA lyase is a promiscuous carbon-carbon bond lyase that catalyzes the reversible cleavage of structurally related CoA thioesters
-
-
?
additional information
?
-
-
the enzyme also catalzes the reversible cleavage of (S)-citramalyl-CoA to acetyl-CoA and pyruvate, reaction of EC 4.1.3.25. Malyl-CoA lyase is a promiscuous carbon-carbon bond lyase that catalyzes the reversible cleavage of structurally related CoA thioesters
-
-
?
additional information
?
-
Chloroflexus aurantiacus OK-70-fl / DSM 636
the enzyme also catalzes the reversible cleavage of (S)-citramalyl-CoA to acetyl-CoA and pyruvate, reaction of EC 4.1.3.25. Malyl-CoA lyase is a promiscuous carbon-carbon bond lyase that catalyzes the reversible cleavage of structurally related CoA thioesters
-
-
?
additional information
?
-
-
the role in C1 metabolism, in organisms utilizing the Ser pathway, may be to provide the glyoxylate necessary to sustain operations of this pathway
-
-
?
additional information
?
-
-
the role in C1 metabolism, in organisms utilizing the Ser pathway, may be to provide the glyoxylate necessary to sustain operations of this pathway
-
-
?
additional information
?
-
-
the enzyme may serve as a route to Gly during biosynthesis of purines and proteins
-
-
?
additional information
?
-
-
the role in C1 metabolism, in organisms utilizing the Ser pathway, may be to provide the glyoxylate necessary to sustain operations of this pathway
-
-
?
additional information
?
-
-
the role in C1 metabolism, in organisms utilizing the Ser pathway, may be to provide the glyoxylate necessary to sustain operations of this pathway
-
-
?
additional information
?
-
Pseudomonas methanolica
-
the enzyme may serve as a route to Gly during biosynthesis of purines and proteins
-
-
?
additional information
?
-
-
the specific activity of malyl-CoA lyase is severalfold higher when grown on C1 compounds than when grown on C2, C3 or C4 compounds
-
-
?
additional information
?
-
-
the specific activity of malyl-CoA lyase is severalfold higher when grown on C1 compounds than when grown on C2, C3 or C4 compounds
-
-
?
additional information
?
-
-
the specific activity of malyl-CoA lyase is severalfold higher when grown on C1 compounds than when grown on C2, C3 or C4 compounds
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
Mn2+
Zn2+
-
divalent cation required, 41% of the activation with Mg2+ and Co2+
Mg2+
required, binding structure, coordination by Glu141 and Asp168, overview
Mg2+
required, binding structure, coordination by Glu157 and Asp184, overview
Mg2+
-
divalent cation required, Mg2+ or Co2+ is most effective
Mn2+
-
divalent cation required, 88% of the activation with Mg2+ and Co2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glycolate
-
in direction of malyl-CoA synthesis: competitive with respect to glyoxylate and noncompetitive with respect to acetyl-CoA.In direction of malyl-CoA cleavage: competitive with respect to malyl-CoA
oxylate
-
in direction of malyl-CoA cleavage: competitive with respect to malyl-CoA
propionyl-CoA
-
in direction of malyl-CoA synthesis: uncompetitive with respect to glyoxylate and competitive with respect to acetyl-CoA. In direction of malyl-CoA cleavage: noncompetitive with respect to malyl-CoA
acetyl-CoA
-
in direction of malyl-CoA cleavage: noncompetitive with respect to malyl-CoA
oxalate
-
in direction of malyl-CoA synthesis: competitive with respect to glyoxylate and noncompetitive with respect to acetyl-CoA. In direction of malyl-CoA cleavage: competitive with respect to malyl-CoA
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.1
glyoxylate
condensation of acetyl-CoA and glyoxylate, at 30°C
4.1
glyoxylate
condensation of propionyl-CoA and glyoxylate, at 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 10
-
pH 6.5: about 55% of maximal activity, pH 10.0: about 45% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Chloroflexus aurantiacus OK-70-fl / DSM 636
strain AM1, i.e. Pseudomonas sp. strain AM1, a mutant of strain AM1 lacking the enzyme
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
malyl-CoA lyase activity is 20fold upregulated in acetate-grown cells versus glucose-grown cells
brenda
-
malyl-CoA lyase activity is 20fold upregulated in acetate-grown cells versus glucose-grown cells
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
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
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
-
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)
-
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
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
-
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
-
physiological function
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
-
the enzyme plays a crucial, multifunctional role in the 3-hydroxypropionate bi-cycle for autotrophic CO2 fixation in 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
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
-
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
-
Show AA Sequence and Transmembrane Helices (691 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36800
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
36800
6 * 36800, 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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
homohexamer
hexamer
6 * 36800, 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
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
hexamer
Chloroflexus aurantiacus OK-70-fl / DSM 636
-
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
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His10-tagged enzyme alone or in complex with substrate propionyl-CoA, inhibitor oxalate, and magnesium ions, pH 7.5, X-ray diffraction structure determination and analysis at 2.5 A resolution, molecular replacement
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
sitting drop vapor diffusion method, using 0.1 M HEPES pH 7.5, 30%(w/v) PEG 400, 0.2 M MgCl2
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography and Superdex 200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into pET16b and expressed as an N-terminal deca-His tag fusion protein in Escherichia coli BL21(DE3) cells
phylogenetic analysis, recombinant expression in Escherichia coli
phylogenetic analysis, recombinant expression of His10-tagged enzyme in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
2.4-fold induction during growth on ethylamine
2.4-fold induction during growth on ethylamine
Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
-
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hersh, L.B.
Malate adenosine triphosphate lyase. Separation of the reaction into a malate thiokinase and malyl coenzyme A lyase
J. Biol. Chem.
248
7295-7303
1973
Pseudomonas sp.
brenda
Tuboi, S.; Kikuchi, G.
Enzymic cleavage of malyl-coenzyme A into acetyl-coenzyme A and glyoxylic acid
Biochim. Biophys. Acta
96
148-153
1965
Cereibacter sphaeroides
brenda
Fulton, G.L.; Nunn, D.N.; Lidstrom, M.E.
Molecular cloning of a malyl coenzyme A lyase gene from Pseudomonas sp. strain AM1, a facultative methylotroph
J. Bacteriol.
160
718-723
1984
Methylorubrum extorquens
brenda
Hacking, A.J.; Quayle, J.R.
Purification and properties of malyl-coenzyme A lyase from Pseudomonas AM1
Biochem. J.
139
399-405
1974
Methylorubrum extorquens, Pseudomonas sp.
brenda
Hersh, L.B.
Malyl coenzyme A lyase. Mechanism of action as deduced by kinetic analysis
J. Biol. Chem.
249
5208-5212
1974
Pseudomonas sp.
brenda
Lynch, M.J.; Wopat, A.E.; O'Connor, M.L.
Characterization of two new facultative methanotrophs
Appl. Environ. Microbiol.
40
400-407
1980
Methylobacterium hypolimneticum, Methylobacterium methanolicum
brenda
Salem, A.R.; Hacking, A.J.; Quayle, J.R.
Cleavage of malyl-Coenzyme A into acetyl-Coenzyme A and glyoxylate by Pseudomonas AM1 and other C1-unit-utilizing bacteria
Biochem. J.
136
89-96
1973
Hyphomicrobium sp., Methylorubrum extorquens, Methylococcus capsulatus, Methylosinus trichosporium, Pseudomonas sp., Pseudomonas methanolica, Pseudomonas sp. MS, Pseudomonas sp. MA, Hyphomicrobium sp. X
brenda
Salem, A.R.; Hacking, A.J.; Quayle, J.R.
Lack of malyl-CoA lyase in a mutant of Pseudomonas AM1
J. Gen. Microbiol.
81
525-527
1974
Methylorubrum extorquens
brenda
Hacking, A.J.; Quayle, J.R.
Malyl-CoA lyase from Methylobacterium extorquens AM1
Methods Enzymol.
188
379-391
1990
Methylorubrum extorquens
-
brenda
Arps, P.J.; Fulton, G.F.; Minnich, E.C.; Lidstrom, M.E.
Genetics of serine pathway enzymes in Methylobacterium extorquens AM1: phosphoenolpyruvate carboxylase and malyl coenzyme A lyase
J. Bacteriol.
175
3776-3783
1993
Methylorubrum extorquens
brenda
Herter, S.; Farfsing, J.; Gad'On, N.; Rieder, C.; Eisenreich, W.; Bacher, A.; Fuchs, G.
Autotrophic CO(2) fixation by Chloroflexus aurantiacus: study of glyoxylate formation and assimilation via the 3-hydroxypropionate cycle
J. Bacteriol.
183
4305-4316
2001
Chloroflexus aurantiacus, Chloroflexus aurantiacus OK-70-fl / DSM 636
brenda
Herter, S.; Busch, A.; Fuchs, G.
L-Malyl-coenzyme A lyase/beta-methylmalyl-coenzyme A lyase from Chloroflexus aurantiacus, a bifunctional enzyme involved in autotrophic CO(2) fixation
J. Bacteriol.
184
5999-6006
2002
Chloroflexus aurantiacus
brenda
Meister, M.; Saum, S.; Alber, B.E.; Fuchs, G.
L-Malyl-coenzyme A/beta-methylmalyl-coenzyme A lyase is involved in acetate assimilation of the isocitrate lyase-negative bacterium Rhodobacter capsulatus
J. Bacteriol.
187
1415-1425
2005
Rhodobacter capsulatus
brenda
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
J. Bacteriol.
192
1249-1258
2010
Cereibacter sphaeroides (Q3J5L6), Cereibacter sphaeroides
brenda
Okubo, Y.; Yang, S.; Chistoserdova, L.; Lidstrom, M.E.
Alternative route for glyoxylate consumption during growth on two-carbon compounds by Methylobacterium extorquens AM1
J. Bacteriol.
192
1813-1823
2010
Methylorubrum extorquens, Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
brenda
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
BMC Struct. Biol.
13
28
2013
Cereibacter sphaeroides (Q3J5L6), Cereibacter sphaeroides, Chloroflexus aurantiacus (S5N020), Chloroflexus aurantiacus, Chloroflexus aurantiacus OK-70-fl / DSM 636 (S5N020)
brenda
Gonzalez, J.M.; Marti-Arbona, R.; Chen, J.C.; Unkefer, C.J.
Structure of Methylobacterium extorquens malyl-CoA lyase CoA-substrate binding correlates with domain shift
Acta Crystallogr. Sect. F
73
79-85
2017
Methylorubrum extorquens (C5B113), Methylorubrum extorquens
brenda
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