Information on EC 4.1.1.47 - Tartronate-semialdehyde synthase

New: Word Map on EC 4.1.1.47
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY hide
4.1.1.47
-
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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
-
-
-
-
decarboxylation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
glycolate and glyoxylate degradation
-
-
glycolate and glyoxylate degradation I
-
-
Glyoxylate and dicarboxylate metabolism
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
glyoxylate carboxy-lyase (dimerizing; tartronate-semialdehyde-forming)
A flavoprotein.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-24-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 83
-
-
Manually annotated by BRENDA team
strain 83
-
-
Manually annotated by BRENDA team
basonym Alcaligenes eutrophus; strain H16
-
-
Manually annotated by BRENDA team
strain H16
-
-
Manually annotated by BRENDA team
strain OX1
-
-
Manually annotated by BRENDA team
strain OX1
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
Gloeomonas sp.
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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
?
-
-
the enzyme is unreactive with 2-ketoacids
-
-
-
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
-
reconstitution of the apoenzyme with 50% recovery of the ativity, Km: 0.00071
5-deaza-FAD
-
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.06
-
mutant enzyme L478A, in 50 mM KH2PO4 (pH 7.7), 0.06 M KCl, 0.1 mM thiamin diphosphate, 5 mM MgCl2, at 37°C
0.68
-
mutant enzyme I393A, in 50 mM KH2PO4 (pH 7.7), 0.06 M KCl, 0.1 mM thiamin diphosphate, 5 mM MgCl2, at 37°C
0.84
-
mutant enzyme I479V, in 50 mM KH2PO4 (pH 7.7), 0.06 M KCl, 0.1 mM thiamin diphosphate, 5 mM MgCl2, at 37°C
0.93
-
mutant enzyme I393V, in 50 mM KH2PO4 (pH 7.7), 0.06 M KCl, 0.1 mM thiamin diphosphate, 5 mM MgCl2, at 37°C
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
7 - 7.7
-
-
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
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
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
-
nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Nicotiana tabacum cultivar Petit Havana
-
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
-
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
-
the mutation leads to a lower catalytic efficiency (5.3%) compared to the wild type enzyme
I479V
-
the mutation leads to a lower catalytic efficiency (4.8%) compared to the wild type enzyme
L478A
-
the mutation leads to a lower catalytic efficiency (0.34%) compared to the wild type enzyme
V51D/I393A
-
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
-
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
Show AA Sequence (1208 entries)
Please use the Sequence Search for a certain query.