Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 4.1.1.47 - tartronate-semialdehyde synthase and Organism(s) Escherichia coli and UniProt Accession P0AEP7

for references in articles please use BRENDA:EC4.1.1.47
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.47 tartronate-semialdehyde synthase
IUBMB Comments
A flavoprotein.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P0AEP7
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
glyoxylate carboligase, tartronate semialdehyde synthase, glyoxalate carboligase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Glyoxalate carboligase
-
-
-
-
Glyoxylate carbo-ligase
-
-
-
-
Glyoxylate carboligase
Glyoxylate carboxy-lyase
-
-
-
-
Glyoxylate carboxy-lyase (dimerizing and reducing)
-
-
-
-
Glyoxylic carbo-ligase
-
-
-
-
Hydroxymalonic semialdehyde carboxylase
-
-
-
-
Synthase, tartronate semialdehyde
-
-
-
-
Tartronate semialdehyde carboxylase
-
-
-
-
Tartronate-semialdehyde synthase
-
-
-
-
Tartronic semialdehyde carboxylase
-
-
-
-
Tartronic semialdehyde synthase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
condensation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
glyoxylate carboxy-lyase (dimerizing; tartronate-semialdehyde-forming)
A flavoprotein.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-24-1
-
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
Tartronate semialdehyde + CO2
show the reaction diagram
additional information
?
-
-
the enzyme is unreactive with 2-ketoacids
-
-
?
NATURAL SUBSTRATE
NATURAL 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
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
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
0.2
-
mutant enzyme V51D, 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
17.5
-
wild type enzyme, in 50 mM KH2PO4 (pH 7.7), 0.06 M KCl, 0.1 mM thiamin diphosphate, 5 mM MgCl2, at 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.7
-
-
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
145000
-
gel filtration
64738
-
x * 64738, calculation from DNA sequence
66000
-
x * 66000, SDS-PAGE
68000
-
2 * 68000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 68000, SDS-PAGE
PROTEIN VARIANTS
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HiTrap Chelating Ni column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Nicotiana tabacum cultivar Petit Havana
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cromartie, T.H.; Walsh, C.T.
Escherichia coli glyoxalate carboligase
J. Biol. Chem.
251
329-333
1976
Escherichia coli
Manually annotated by BRENDA team
Gupta, N.K.; Vennesland, B.
Glyoxylate carboligase of Escherichia coli: a flavoprotein
J. Biol. Chem.
239
3787-3789
1964
Escherichia coli
Manually annotated by BRENDA team
Chang, Y.Y.; Wang, A.Y.; Cronan, J.E.
Molecular cloning, DNA sequencing, and biochemical analyses of Escherichia coli glyoxylate carboligase
J. Biol. Chem.
268
3911-3919
1993
Escherichia coli
Manually annotated by BRENDA team
Shaanan, B.; Chipman, D.M.
Reaction mechanisms of thiamin diphosphate enzymes: new insights into the role of a conserved glutamate residue
FEBS J.
276
2447-2453
2009
Escherichia coli
Manually annotated by BRENDA team
Nemeria, N.; Binshtein, E.; Patel, H.; Balakrishnan, A.; Vered, I.; Shaanan, B.; Barak, Z.; Chipman, D.; Jordan, F.
Glyoxylate carboligase: a unique thiamin diphosphate-dependent enzyme that can cycle between the 4'-aminopyrimidinium and 1,4'-iminopyrimidine tautomeric forms in the absence of the conserved glutamate
Biochemistry
51
7940-7952
2012
Escherichia coli
Manually annotated by BRENDA team
Carvalho, J.d.e..F.; Madgwick, P.J.; Powers, S.J.; Keys, A.J.; Lea, P.J.; Parry, M.A.
An engineered pathway for glyoxylate metabolism in tobacco plants aimed to avoid the release of ammonia in photorespiration
BMC Biotechnol.
11
111
2011
Escherichia coli
Manually annotated by BRENDA team