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Information on EC 4.1.1.85 - 3-dehydro-L-gulonate-6-phosphate decarboxylase
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EC Tree
4.1.1.85 3-dehydro-L-gulonate-6-phosphate decarboxylaseIUBMB Comments
Requires Mg2+. Along with EC 5.1.3.22, L-ribulose-5-phosphate 3-epimerase, this enzyme is involved in a pathway for the utilization of L-ascorbate by Escherichia coli.
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Word Map
- 4.1.1.85
- ompdc
- orotidine
-
5'-monophosphate
-
suprafamily
-
mg2+-dependent
-
enediolate
- l-ascorbate
-
gerlt
-
wise
-
beta-strands
-
cis-enediolate
-
rayment
- d-ribulose
- ump
-
bidentate
- d-xylulose
-
babbitt
-
ion-independent
-
vinyl
-
3-epimerase
-
conscripting
-
methylomonas
-
hydrogen-bonded
- lys
- 4-phosphate
-
manuscript
-
relay
-
bacteriol
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
kgpdc, 3-keto-l-gulonate 6-phosphate decarboxylase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-keto-L-gulonate 6-phosphate decarboxylase
KGPDC
additional information
additional information
the enzyme belongs to the orotidine 5'-monophosphate decarboxylase OMPDC suprafamily
additional information
the enzyme belongs to the orotidine 5'-monophosphate decarboxylase OMPDC suprafamily, overview
additional information
the enzyme belongs to the orotidine 5'-monophosphate decarboxylase OMPDC suprafamily, overview
additional information
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the enzyme belongs to the orotidine 5'-monophosphate decarboxylase OMPDC suprafamily
additional information
-
the enzyme belongs to the orotidine 5'-monophosphate decarboxylase OMPDC suprafamily
additional information
the enzyme belongs to the orotidine 5'-monophosphate decarboxylase OMPDC suprafamily
additional information
-
the enzyme belongs to the orotidine 5'-monophosphate decarboxylase OMPDC suprafamily
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-dehydro-L-gulonate 6-phosphate + H+ = L-xylulose 5-phosphate + CO2
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-
-
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3-dehydro-L-gulonate 6-phosphate + H+ = L-xylulose 5-phosphate + CO2
active site structure, substrate binding structure, formation of a cis-1,2-enediolate anion intermediate, intermediate structure and reaction mechanism involving residues Lys64, Asp67, and His136, overview
3-dehydro-L-gulonate 6-phosphate + H+ = L-xylulose 5-phosphate + CO2
active site structure, substrate binding structure, structure-function relationship, overview
3-dehydro-L-gulonate 6-phosphate + H+ = L-xylulose 5-phosphate + CO2
catalytic mechanism, formation and Mg2+-stabilization of an cis-1,2-enediolate anion intermediate, important residues for the stereospecific exchange of the pro-1S hydrogen are Lys64, Asp67, Glu112, Arg139, and Lys64, the latter stabilizes the intermediate via hydrogen bonds to O1 and O2 of the intermediate involving conserved active site residue Asp67, His136 takes part in hydrogen exchange with solvent of the 1-hydroxymethylene group of the product, overview
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3-dehydro-L-gulonate 6-phosphate + H+ = L-xylulose 5-phosphate + CO2
formation and stabilization of an 1,2-enediolate anion intermediate, protonation of the intermediate involving residues Glu112, His136, and Arg139, active site structure-function relationship, overview
3-dehydro-L-gulonate 6-phosphate + H+ = L-xylulose 5-phosphate + CO2
formation and stabilization of an enediolate anion intermediate is part of reaction mechanism, mechanism overview, the active site is located at the dimer interface, structure-function relationship, overview
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
3-dehydro-L-gulonate-6-phosphate carboxy-lyase (L-xylulose-5-phosphate-forming)
Requires Mg2+. Along with EC 5.1.3.22, L-ribulose-5-phosphate 3-epimerase, this enzyme is involved in a pathway for the utilization of L-ascorbate by Escherichia coli.
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CAS REGISTRY NUMBER
COMMENTARY
406722-60-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-dehydro-L-gulonate 6-phosphate + H+
L-xylulose 5-phosphate + CO2
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-
-
-
?
3-dehydro-L-gulonate 6-phosphate + H+
L-xylulose 5-phosphate + CO2
-
-
-
?
3-dehydro-L-gulonate 6-phosphate + H+
L-xylulose 5-phosphate + CO2
substrate binding structure
-
-
?
3-dehydro-L-gulonate 6-phosphate + H+
L-xylulose 5-phosphate + CO2
-
-
-
?
3-dehydro-L-gulonate 6-phosphate + H+
L-xylulose 5-phosphate + CO2
-
stereochemistry
-
-
?
3-dehydro-L-gulonate 6-phosphate + H+
L-xylulose 5-phosphate + CO2
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SgaH/UlaD and SgbH
-
-
?
3-dehydro-L-gulonate 6-phosphate + H+
L-xylulose 5-phosphate + CO2
-
step in the catabolic pathway of L-ascorbate utilization
-
-
?
3-dehydro-L-gulonate 6-phosphate + H+
L-xylulose 5-phosphate + CO2
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-
-
-
?
additional information
?
-
-
enzyme catalyzes one step in the L-ascorbate utilization pathway, L-ascorbate is converted to L-xylulose, overview
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-
?
additional information
?
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enzymes SgaH/UlaD and SgbH are not active with 3-dehydro-L-gulonate
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-
?
additional information
?
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the enzyme also performs the Methylomonas aminofaciens D-arabino-hex-3-ulose 6-phosphate synthase reaction with low activity catalyzing Mg2+-dependent aldol condensation between formaldehyde and D-ribulose 5-phosphate, while the Methylomonas aminofaciens enzyme also performs the 3-keto-L-gulonate 6-phosphate decarboxylase reaction, overview
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-
?
additional information
?
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-
the enzyme also performs the Methylomonas aminofaciens D-arabino-hex-3-ulose 6-phosphate synthase reaction with low activity catalyzing Mg2+-dependent aldol condensation between formaldehyde and D-ribulose 5-phosphate, while the Methylomonas aminofaciens enzyme also performs the 3-keto-L-gulonate 6-phosphate decarboxylase reaction, proton exchange reaction rates, overview
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-
?
additional information
?
-
-
the D-arabino-hex-3-ulose 6-phosphate synthase of Methylomonas aminofaciens also performs the 3-keto-L-gulonate 6-phosphate decarboxylase reaction with lower activity than for the preferred reaction catalyzing Mg2+-dependent aldol condensation between formaldehyde and D-ribulose 5-phosphate, proton exchange reaction rates, overview
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
enzyme catalyzes one step in the L-ascorbate utilization pathway, L-ascorbate is converted to L-xylulose, overview
-
-
?
3-dehydro-L-gulonate 6-phosphate + H+
L-xylulose 5-phosphate + CO2
-
-
-
?
3-dehydro-L-gulonate 6-phosphate + H+
L-xylulose 5-phosphate + CO2
-
-
-
?
3-dehydro-L-gulonate 6-phosphate + H+
L-xylulose 5-phosphate + CO2
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SgaH/UlaD and SgbH
-
-
?
3-dehydro-L-gulonate 6-phosphate + H+
L-xylulose 5-phosphate + CO2
-
step in the catabolic pathway of L-ascorbate utilization
-
-
?
3-dehydro-L-gulonate 6-phosphate + H+
L-xylulose 5-phosphate + CO2
-
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
dependent on, binding structure involving Glu33 and Asp62, overview
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-gulonate 6-phosphate
binding structure involving Glu33 and Asp62 and Mg2+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
analysis of kinetics and activity of the mutant enzymes, overview
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0.15
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant E112Q/H136A
0.22
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant E112Q/H136A/R139V
0.27
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant D67A/H136A
0.3
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutants K64R and D67N/H136A
0.31
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant E112Q
0.34
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant E112A
0.36
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant R139V
0.37
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant H136N
0.41
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant D67N
0.44
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant K64R/H136A
0.5
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant D67A
0.51
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant K64A
0.52
3-dehydro-L-gulonate 6-phosphate
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pH 7.5, 25°C, recombinant mutant H136Q
0.55
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant K64A/E112Q/H136A
0.58
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant K64A/H136A
0.65
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant E112A/H136A
0.67
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant wild-type enzyme
0.7
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant H136A
0.77
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant E112A/H136A/R139V
0.9
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant K64A/R139V
0.91
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant E112D/R139V/T169A
1.4
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutants H136A/R139V and K64A/E112A/H136A/R139V
5.4
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.19
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant D67A/H136A
0.2
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant E112Q/H136A/R139V
0.21
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant E112A/H136A/R139V
0.23
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant E112Q/H136A
0.26
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant K64A/E112A/H136A/R139V
0.3
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant E112A
0.45
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant E112A/H136A
0.75
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant K64A/H136A
1.1
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant D67N
1.2
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant K64A/R139V
1.3
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant D67N/H136A
1.4
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant H136Q
2.4
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant E112D/R139V/T169A
2.4
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutants D67A and H136A
2.9
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant K64A/E112Q/H136A
4
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant E112Q
4.2
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant K64R/H136A
4.3
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant H136N
8.3
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant K64A
8.9
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant R139V
9.2
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant H136A/R139V
15
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant enzyme
17
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant mutant K64R
51
3-dehydro-L-gulonate 6-phosphate
-
pH 7.5, 25°C, recombinant wild-type enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene ulaD or sgaH encoded in the yia-sga operon, and gene sgbH encoded in the yia-sgb operon
-
-
brenda
Show AA Sequence and Transmembrane Helices (1431 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
dimer
(beta/alpha)8-barrel enzyme, the active site is located at the dimer interface
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme complexed with L-gulonate 6-phosphate, L-threonohydroxamate 4-phosphate, and L-xylitol 5-phosphate, analogues of the substrate, enediolate intermediate, and product, as well as with the product L-xylulose 5-phosphate, 15 mg/ml protein in 50 mM HEPES, pH 7.5, 5 mM MgCl2, 100 mM NaCl, micro-batch method, 0.01 ml protein solution mixed with equal volume of crystallization solution containing 16% monomethyl PEG 5000, 100 mM Bis-Tris propane, pH 7.0, and 5 mM MgCl2, with 25 mM ligand, X-ray diffraction structure determination and analysis at 1.2, 1.8, 1.7, and 1.8 A resolution, respectively
purified recombinant mutant enzymes K64A, H136A, E112Q, and E112Q/H136A, in complex with reaction intermediate analogue L-threonohydroxamate 4-phosphate, 15 mg/ml protein in 50 mM HEPES, pH 7.5, 5 mM MgCl2, 100 mM NaCl, 0.01 ml protein solution mixed with equal volume of crystallization solution containing 16% monomethyl PEG 5000, 100 mM Bis-Tris propane, pH 7.0, 5 mM MgCl2, and 25 mM L-threonohydroxamate 4-phosphate, X-ray diffraction structure determination and analysis at 1.7, 1.9, 1.8, and 1.9 A resolution, respectively
purified recombinant wild-type and selenomethionine-labeled enzymes, free or complexed with inhibitor L-gulonate 6-phosphate, 15 mg/ml protein in 50 mM HEPES, pH 7.5, 5 mM MgCl2, 100 mM NaCl, room temperature, micro-batch method, 0.01 ml protein solution mixed with equal volume of crystallization solution containing 18% monomethyl PEG 5000, 50 mM NaH2PO4, 50 mM K2HPO4, and 50 mM Bis-Tris propane, pH 7.0, with or without 20 mM inhibitor L-gulonate 6-phosphate, crystals appear a few days after microseeding, growing for 1 week, X-ray diffraction structure determination and analysis at 2.0 A resolution
purified recombinant wild-type and mutant enzymes E112D/R139V, E112D/T169A, and E112D/R139V/T169A, 15 mg/ml protein in 50 mM HEPES, pH 7.5, 5 mM MgCl2, 100 mM NaCl, micro-batch method, 0.01 ml protein solution mixed with equal volume of crystallization solution containing 16% monomethyl PEG 5000, 100 mM Bis-Tris propane, pH 7.0, 5 mM MgCl2, and 25 mM L-xylulose 5-phosphate or D-ribulose 5-phosphate, cryoprotection of crystals in 15% monomethylPEG 5000, 100 mM PIPES, pH 7.0, 15% ethylene glycol, 200 mM NaCl, and 50 mM L-threonohydroxamate 4-phosphate or 50 mM D-ribulose 5-phosphate, X-ray diffraction structure determination and analysis at 1.6-1.8 A resolution, molecular replacement
at 289 K using the hanging-drop vapor-diffusion technique. Apoenzyme obtained in two different space groups P212121 (without Mg2+) and I422 (in complex with Mg2+) and in the absence and presence of the product analog D-ribulose 5-phosphate. An 8 A alphaB-helix movement and other structural rearrangements around the active site between the apostructures and product analog bound structure. Conformational flexibility around the active site for substrate/product binding. Especially the alphaB-helix (residues 144-149) and the side chains of the conserved Arg144 and Arg197 exhibit openclosed conformational changes between the apo-structure and complex structure with ligand bound at the active site
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E112Q
site-directed mutagenesis, crystal structure determination and analysis, the mutant enzyme shows altered reaction intermediate binding at the active site, reaction mechanism, and stereochemistry
E112Q/H136A
site-directed mutagenesis, crystal structure determination and analysis, the mutant enzyme shows altered reaction intermediate binding at the active site, reaction mechanism, and stereochemistry
H136A
site-directed mutagenesis, crystal structure determination and analysis, the mutant enzyme shows altered reaction intermediate binding at the active site, reaction mechanism, and stereochemistry
K64A
site-directed mutagenesis, crystal structure determination and analysis, the mutant enzyme shows altered reaction intermediate binding at the active site, reaction mechanism, and stereochemistry
D67A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
D67A/H136A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
D67N
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
D67N/H136A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
E112A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
E112A/H136A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
E112A/H136A/R139V
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
E112D/R139V
site-directed mutagenesis, mutations alter the Escherichia coli residues to those of Methylomonas aminofaciens D-arabino-hex-3-ulose 6-phosphate synthase, a homologous enzyme, also altering the enzyme activity of the 3-keto-L-gulonate 6-phosphate decarboxylase performing th Mg2+-dependent aldol condensation between formaldehyde and D-ribulose 5-phosphate with highly increased activity compared to the wild-type enzyme
E112D/R139V/T169A
E112D/R139V/T169A/R192A
-
site-directed mutagenesis, mutations alter the Escherichia coli residues to those of Methylomonas aminofaciens D-arabino-hex-3-ulose 6-phosphate synthase, a homologous enzyme, also altering the enzyme activity of the 3-keto-L-gulonate 6-phosphate decarboxylase performing th Mg2+-dependent aldol condensation between formaldehyde and D-ribulose 5-phosphate with highly increased activity compared to the wild-type enzyme
E112D/T169A
site-directed mutagenesis, mutations alter the Escherichia coli residues to those of Methylomonas aminofaciens D-arabino-hex-3-ulose 6-phosphate synthase, a homologous enzyme, also altering the enzyme activity of the 3-keto-L-gulonate 6-phosphate decarboxylase performing th Mg2+-dependent aldol condensation between formaldehyde and D-ribulose 5-phosphate with highly increased activity compared to the wild-type enzyme
E112Q
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
E112Q/H136A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
E112Q/H136A/R139V
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
H136A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
H136A/R139V
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
H136N
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
H136Q
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
K64A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
K64A/E112A/H136A/R139V
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
K64A/E112Q/H136A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
K64A/H136A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
K64A/R139V
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
K64R
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
K64R/H136A
-
site-directed mutagenesis, reduced activity compared to the wild-type enzyme
R139V
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme
E112D/R139V/T169A
-
site-directed mutagenesis, mutations alter the Escherichia coli residues to those of Methylomonas aminofaciens D-arabino-hex-3-ulose 6-phosphate synthase, a homologous enzyme, also altering the enzyme activity of the 3-keto-L-gulonate 6-phosphate decarboxylase performing th Mg2+-dependent aldol condensation between formaldehyde and D-ribulose 5-phosphate with highly increased activity compared to the wild-type enzyme
E112D/R139V/T169A
site-directed mutagenesis, mutations alter the Escherichia coli residues to those of Methylomonas aminofaciens D-arabino-hex-3-ulose 6-phosphate synthase, a homologous enzyme, also altering the enzyme activity of the 3-keto-L-gulonate 6-phosphate decarboxylase performing th Mg2+-dependent aldol condensation between formaldehyde and D-ribulose 5-phosphate with highly increased activity compared to the wild-type enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged UlaD from strain BL21(DE3), the His-tag is removed by thrombin
recombinant N-terminally His10-tagged SgbH from strain BL21(DE3) to homogeneity, the His-tag is removed by thrombin
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of N-terminally His10-tagged wild-type and mutant enzymes in enzyme-deficient strain BLR(DE3)
gene sgbH, expression in strain BL21(DE3) as N-terminally His10-tagged protein
-
gene ulaD, expression as His-tagged protein in strain BL21(DE3), and as selenomethionine-labeled enzyme
into pET-28a vector containing an N-terminal His6-tag and expressed in Escherichia coli strain BL21 (DE3) cells
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expression of N-terminally His10-tagged wild-type and mutant enzymes in enzyme-deficient strain BLR(DE3)
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expression of N-terminally His10-tagged wild-type and mutant enzymes in enzyme-deficient strain BLR(DE3)
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expression of N-terminally His10-tagged wild-type and mutant enzymes in enzyme-deficient strain BLR(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wise, E.; Yew, W.S.; Babbitt, P.C.; Gerlt, J.A.; Rayment, I.
Homologous (beta/alpha)8-barrel enzymes that catalyze unrelated reactions: orotidine 5'-monophosphate decarboxylase and 3-keto-L-gulonate 6-phosphate decarboxylase
Biochemistry
41
3861-3869
2002
Escherichia coli (P39304), Escherichia coli
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Wise, E.L.; Yew, W.S.; Gerlt, J.A.; Rayment, I.
Structural evidence for a 1,2-enediolate intermediate in the reaction catalyzed by 3-keto-L-gulonate 6-phosphate decarboxylase, a member of the orotidine 5'-monophosphate decarboxylase suprafamily
Biochemistry
42
12133-12142
2003
Escherichia coli (P39304)
brenda
Yew, W.S.; Wise, E.L.; Rayment, I.; Gerlt, J.A.
Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: mechanistic evidence for a proton relay system in the active site of 3-keto-L-gulonate 6-phosphate decarboxylase
Biochemistry
43
6427-6437
2004
Escherichia coli K-12
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Wise, E.L.; Yew, W.S.; Gerlt, J.A.; Rayment, I.
Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: crystallographic evidence for a proton relay system in the active site of 3-keto-L-gulonate 6-phosphate decarboxylase
Biochemistry
43
6438-6446
2004
Escherichia coli (P39304)
brenda
Yew, W.S.; Akana, J.; Wise, E.L.; Rayment, I.; Gerlt, J.A.
Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: enhancing the promiscuous D-arabino-hex-3-ulose 6-phosphate synthase reaction catalyzed by 3-keto-L-gulonate 6-phosphate decarboxylase
Biochemistry
44
1807-1815
2005
Escherichia coli K-12, Methylomonas aminofaciens
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Wise, E.L.; Yew, W.S.; Akana, J.; Gerlt, J.A.; Rayment, I.
Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: structural basis for catalytic promiscuity in wild-type and designed mutants of 3-keto-L-gulonate 6-phosphate decarboxylase
Biochemistry
44
1816-1823
2005
Escherichia coli K-12 (P39304)
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Yew, W.S.; Gerlt, J.A.
Utilization of L-ascorbate by Escherichia coli K-12: assignments of functions to products of the yjf-sga and yia-sgb operons
J. Bacteriol.
184
302-306
2002
Escherichia coli K-12
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Akana, J.; Fedorov, A.A.; Fedorov, E.; Novak, W.R.; Babbitt, P.C.; Almo, S.C.; Gerlt, J.A.
D-Ribulose 5-phosphate 3-epimerase: functional and structural relationships to members of the ribulose-phosphate binding (beta/alpha)8-barrel superfamily
Biochemistry
45
2493-2503
2006
Escherichia coli
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Li, G.L.; Liu, X.; Nan, J.; Brostromer, E.; Li, L.F.; Su, X.D.
Open-closed conformational change revealed by the crystal structures of 3-keto-L-gulonate 6-phosphate decarboxylase from Streptococcus mutans
Biochem. Biophys. Res. Commun.
381
429-433
2009
Streptococcus mutans, Streptococcus mutans UA159
brenda
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