Information on EC 4.1.3.46 - (R)-citramalyl-CoA lyase

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The expected taxonomic range for this enzyme is: Chloroflexus aurantiacus

EC NUMBER
COMMENTARY hide
4.1.3.46
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RECOMMENDED NAME
GeneOntology No.
(R)-citramalyl-CoA lyase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(3R)-citramalyl-CoA = acetyl-CoA + pyruvate
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
(3R)-citramalyl-CoA pyruvate-lyase (acetyl-CoA-forming)
Requires Mn2+ ions for activity. The enzyme, purified from the bacterium Chloroflexus aurantiacus, has no activity with (3S)-citramalyl-CoA (cf. EC 4.1.3.25, (S)-citramalyl-CoA lyase).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain OK-70-fl
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3R)-citramalyl-CoA
acetyl-CoA + pyruvate
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(3R)-citramalyl-CoA
acetyl-CoA + pyruvate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
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enzyme activity is stimulated by divalent cations in the order Mn2+, Co2+ > Ni2+ > Mg2+
copper
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the recombinant enzyme contains 0.5 mol of zinc per mol of native enzyme. Additionally, 0.2 mol copper per mol native protein and traces of iron are detected
Mg2+
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dependent; enzyme activity is stimulated by divalent cations in the order Mn2+, Co2+ > Ni2+ > Mg2+
Mn2+
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enzyme activity is stimulated by divalent cations in the order Mn2+, Co2+ > Ni2+ > Mg2+. The addition of both 4 mM dithioerythritol and 4 mM Mn2+ enhances the enzyme activity approximately 10fold compared to the results of an assay lacking dithioerythritol and Mn2+
Ni2+
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enzyme activity is stimulated by divalent cations in the order Mn2+, Co2+ > Ni2+ > Mg2+
Zinc
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the recombinant enzyme contains 0.5 mol of zinc per mol of native enzyme. Additionally, 0.2 mol copper per mol native protein and traces of iron are detected
additional information
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no stimulation is obtained after the addition of Ca2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
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activity is completely restored by the addition of excess Mn2+
iodoacetamide
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in the absence of dithiothreitol, the addition of iodoacetamide (4 mM) results in complete loss of activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithioerythritol
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4 mM, enhances the enzyme activity about threefold. The addition of both 4 mM dithioerythritol and 4 mM Mn2+ enhances the enzyme activity approximately 10fold compared to the results of an assay lacking dithioerythritol and Mn2+
additional information
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up-regulated severalfold during autotrophic growth
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07
(3R)-citramalyl-CoA
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pH 7.0, 55°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.7
(3R)-citramalyl-CoA
Chloroflexus aurantiacus
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pH 7.0, 55°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.02
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recombinant enzyme
1.5
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recombinant enzyme
1.52
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pH 7.0, 55°C, purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3 - 7.6
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half-maximal activities at pHs of 6.3 and 7.6
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34000
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2 * 34000, SDS-PAGE
65000
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gel filtration
68000
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SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, pH 7.0, no significant loss of activity
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frozen for months in the presence of 10% glycerol (v/v) without significant loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, gel filtration, and Mono Q chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli; expression in Escherichia coli
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