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2 glyoxylate
tartronate semialdehyde + CO2
Glyoxylate
Tartronate semialdehyde + CO2
additional information
?
-
-
the enzyme is unreactive with 2-ketoacids
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?
2 glyoxylate
tartronate semialdehyde + CO2
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-
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2 glyoxylate
tartronate semialdehyde + CO2
-
-
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?
Glyoxylate
?
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synthesis of the enzyme and thus the degradation of purine derivatives is repressed by high concentrations of adenine
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Glyoxylate
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synthesis of the enzyme and thus the degradation of purine derivatives is repressed by high concentrations of adenine
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?
Glyoxylate
?
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the enzyme is stimulated by light and inhibited during nitrogen starvation, activity is only partially recovered after reintroduction of nitrate
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Glyoxylate
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enzyme of the glyoxylate metabolism
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Glyoxylate
?
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enzyme of the glyoxylate metabolism
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Glyoxylate
Tartronate semialdehyde + CO2
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Glyoxylate
Tartronate semialdehyde + CO2
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?
Glyoxylate
Tartronate semialdehyde + CO2
-
-
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?
Glyoxylate
Tartronate semialdehyde + CO2
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-
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?
Glyoxylate
Tartronate semialdehyde + CO2
-
-
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?
Glyoxylate
Tartronate semialdehyde + CO2
-
-
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?
Glyoxylate
Tartronate semialdehyde + CO2
-
-
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?
Glyoxylate
Tartronate semialdehyde + CO2
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?
Glyoxylate
Tartronate semialdehyde + CO2
-
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?
Glyoxylate
Tartronate semialdehyde + CO2
Gloeomonas sp.
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Glyoxylate
Tartronate semialdehyde + CO2
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?
Glyoxylate
Tartronate semialdehyde + CO2
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?
Glyoxylate
Tartronate semialdehyde + CO2
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?
Glyoxylate
Tartronate semialdehyde + CO2
-
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?
Glyoxylate
Tartronate semialdehyde + CO2
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?
Glyoxylate
Tartronate semialdehyde + CO2
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?
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0.58
glyoxylate
-
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
0.65
glyoxylate
-
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
1.3
glyoxylate
mutant V51D
1.3
glyoxylate
-
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
1.79
glyoxylate
-
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
2.06
glyoxylate
-
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
5.3
glyoxylate
mutant V51E
16.5
glyoxylate
mutant E52Q
17.3
glyoxylate
mutant V51S
21
glyoxylate
wild-type enzyme
21
glyoxylate
-
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
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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
17.1
mutant V51S is nearly as active as the wild-type enzyme
2.7
mutant V51E is about seven times slower than the wild-type enzyme
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
0.2
mutant V51D catalyzes the formation of the product nearly two orders of magnitude more slowly than the wild-type enzyme
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
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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
V51D
-
replacement of Val51 by an amino acid with a carboxylate in its side chain (glutamate or aspartate) has striking and significant effects, V51D variant of glyoxylate carboligase undergoes proton exchange at a rate 6fold higher than the wild-type enzyme
V51D
-
the substitution shifts the pH optimum to 6.0-6.2, the mutant is less active (1.2%) than the wild type enzyme (turnover rates are 2 orders of magnitude lower) despite having higher rate of activation of the coenzyme
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Cromartie, T.H.; Walsh, C.T.
Escherichia coli glyoxalate carboligase
J. Biol. Chem.
251
329-333
1976
Escherichia coli
brenda
Badour, S.S.; Waygood, E.R.
Glyoxylate carboxy-lyase activity in the unicellular green alga Gloeomonas sp.
Biochim. Biophys. Acta
242
493-499
1971
Gloeomonas sp.
brenda
Gupta, N.K.; Vennesland, B.
Glyoxylate carboligase of Escherichia coli: a flavoprotein
J. Biol. Chem.
239
3787-3789
1964
Escherichia coli
brenda
Eschmann, K.; Kaltwasser, H.
Inhibition of purine utilization by adenine in Alcaligenes eutrophus H16
Arch. Microbiol.
125
29-34
1980
Cupriavidus necator, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
brenda
Braun, W.; Kaltwasser, H.
Untersuchungen zum Glyoxylsurestoffwechsel von Bacillus fastidiosus Stamm 83
Arch. Microbiol.
121
129-134
1979
Metabacillus fastidiosus, Metabacillus fastidiosus 83
-
brenda
Dijkhuizen, L.; Knight, M.; Harder, W.
Metabolic regulation in Pseudomonas oxalaticus OX1. Autotrophic and heterotrophic growth on mixed substrates
Arch. Microbiol.
116
77-83
1978
Cupriavidus oxalaticus, Cupriavidus oxalaticus OX1
brenda
Paul, J.S.; Volcani, B.E.
Photorespiration in diatoms. IV. Two pathways of glycolate metabolism in synchronized cultured of Cylindrotheca fusiformis
Arch. Microbiol.
110
247-252
1976
Cylindrotheca fusiformis
brenda
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
brenda
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
brenda
Kaplun, A.; Binshtein, E.; Vyazmensky, M.; Steinmatz, A.; Barak, Z.; Chipman, D.M.; Tittmann, K.; Shaanan, B.
Glyoxylate carboligase lacks the canonical active site glutamate of thiamine-dependent enzymes
Nat. Chem. Biol.
4
113-118
2008
Escherichia coli K-12 (P0AEP7)
brenda
Li, X.Z.; Klebensberger, J.; Rosche, B.
Effect of gcl, glcB and aceA disruption on glyoxylate conversion by Pseudomonas putida JM37
J. Microbiol. Biotechnol.
20
1006-1010
2010
Pseudomonas putida, Pseudomonas putida JM37
brenda
Grostern, A.; Sales, C.M.; Zhuang, W.Q.; Erbilgin, O.; Alvarez-Cohen, L.
Glyoxylate metabolism is a key feature of the metabolic degradation of 1,4-dioxane by Pseudonocardia dioxanivorans strain CB1190
Appl. Environ. Microbiol.
78
3298-3308
2012
Pseudonocardia dioxanivorans, Pseudonocardia dioxanivorans CB1190
brenda
Mueckschel, B.; Simon, O.; Klebensberger, J.; Graf, N.; Rosche, B.; Altenbuchner, J.; Pfannstiel, J.; Huber, A.; Hauer, B.
Ethylene glycol metabolism by Pseudomonas putida
Appl. Environ. Microbiol.
78
8531-8539
2012
Pseudomonas putida, Pseudomonas putida JM37
brenda
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
brenda
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
brenda