Information on EC 4.1.1.47 - Tartronate-semialdehyde synthase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
4.1.1.47
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RECOMMENDED NAME
GeneOntology No.
Tartronate-semialdehyde synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 glyoxylate = 2-hydroxy-3-oxopropanoate + CO2
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
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decarboxylation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
glycolate and glyoxylate degradation I
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glycolate and glyoxylate degradation
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Glyoxylate and dicarboxylate metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
glyoxylate carboxy-lyase (dimerizing; tartronate-semialdehyde-forming)
A flavoprotein.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-24-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
strain 83
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Manually annotated by BRENDA team
strain 83
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
basonym Alcaligenes eutrophus; strain H16
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Manually annotated by BRENDA team
strain H16
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Manually annotated by BRENDA team
strain OX1
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
Gloeomonas sp.
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 glyoxylate
tartronate semialdehyde + CO2
show the reaction diagram
Glyoxylate
?
show the reaction diagram
Glyoxylate
Tartronate semialdehyde + CO2
show the reaction diagram
additional information
?
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the enzyme is unreactive with 2-ketoacids
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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
2 glyoxylate
tartronate semialdehyde + CO2
show the reaction diagram
Glyoxylate
?
show the reaction diagram
Glyoxylate
Tartronate semialdehyde + CO2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,5-Dihydro-5-deaza-FADH2
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reconstitution of the apoenzyme with 50% recovery of the ativity, Km: 0.00071
5-deaza-FAD
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can reconstitute the apoenzyme to full activity, Km: 0.00074 mM
thiamine diphosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2 - 1.2
glyoxylate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.25 - 19.7
glyoxylate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.58 - 21
glyoxylate
101
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.06
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mutant enzyme L478A, in 50 mM KH2PO4 (pH 7.7), 0.06 M KCl, 0.1 mM thiamin diphosphate, 5 mM MgCl2, at 37C
0.68
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mutant enzyme I393A, in 50 mM KH2PO4 (pH 7.7), 0.06 M KCl, 0.1 mM thiamin diphosphate, 5 mM MgCl2, at 37C
0.84
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mutant enzyme I479V, in 50 mM KH2PO4 (pH 7.7), 0.06 M KCl, 0.1 mM thiamin diphosphate, 5 mM MgCl2, at 37C
0.93
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mutant enzyme I393V, in 50 mM KH2PO4 (pH 7.7), 0.06 M KCl, 0.1 mM thiamin diphosphate, 5 mM MgCl2, at 37C
2.7
mutant V51E is about seven times slower than the wild-type enzyme
17.1
mutant V51S is nearly as active as the wild-type enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
145000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 68000, SDS-PAGE
homotetramer
the apparent functional unit is a dimer with a pair of identical thiamine diphosphate binding sites at the dimer interface
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glyoxylate carboligase crystallizes with 6 monomers (a tetramer and a dimer) in an asymmetric unit, vapor diffusion hanging-drop, 2-4 microlitre of protein solution (5-15 mg/ml, 100 micromolar ThDP, 10 micromolar FAD, 1mM MgCl2 and 10 mM quinone Q0) are mixed with equal volume of reservoir solution (0.5% PEG6000, 0.5M NaCl, 40 mM DTT), pH 8.00, temperature 294K, space group P41212, resolution 2.70 A
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HiTrap Chelating Ni column chromatography
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nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Nicotiana tabacum cultivar Petit Havana
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expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in ethylene glycol-treated cells glyoxylate carboligase expression is induced 9.6fold
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
I393A
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the mutation leads to a lower catalytic efficiency (3.9%) compared to the wild type enzyme. The enzyme is converted to an acetolactate synthase which can use pyruvate as a substrate with a catalytic efficiency (kcat/Km) of about 20times higher than that of the wild type enzyme
I393V
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the mutation leads to a lower catalytic efficiency (5.3%) compared to the wild type enzyme
I479V
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the mutation leads to a lower catalytic efficiency (4.8%) compared to the wild type enzyme
L478A
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the mutation leads to a lower catalytic efficiency (0.34%) compared to the wild type enzyme
V51D/I393A
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the enzyme is converted to an acetolactate synthase which can use pyruvate as a substrate with a catalytic efficiency (kcat/Km) of about 20times higher than that of the wild type enzyme
V51E
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the mutant is less active than the wild type enzyme (turnover rates are 7fold lower) despite having higher rate of activation of the coenzyme
E52Q
site-directed mutagenesis
V51D
site-directed mutagenesis
V51E
site-directed mutagenesis
V51S
site-directed mutagenesis
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