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Information on EC 4.1.2.14 - 2-dehydro-3-deoxy-phosphogluconate aldolase and Organism(s) Escherichia coli and UniProt Accession P0A955
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4.1.2.14 2-dehydro-3-deoxy-phosphogluconate aldolaseIUBMB Comments
The enzyme shows no activity with 2-dehydro-3-deoxy-6-phosphate-D-galactonate. cf. EC 4.1.2.55, 2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase . Also acts on 2-oxobutanoate .
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Word Map
- 4.1.2.14
-
entner-doudoroff
- dehydratase
- aldolases
- bromopyruvate
-
pectinolytic
-
carbinolamine
- 2-keto-3-deoxy-6-phosphogalactonate
- synthesis
-
embden-meyerhof-parnas
-
schiff-base
-
embden-meyerhof
- medicine
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
2-keto-3-deoxy-6-phosphogluconate aldolase, kdpg aldolase, phospho-2-keto-3-deoxygluconate aldolase, kdpga, kd(p)g aldolase, kdpg-aldolase, 2-dehydro-3-deoxy-phosphogluconate aldolase, 6-phospho-2-keto-3-deoxygluconate aldolase, 2-keto-3-deoxygluconate-6-phosphate aldolase, 2-dehydro-3-deoxyphosphogluconate aldolase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-dehydro-3-deoxyphosphogluconate aldolase
-
-
-
-
2-keto-3-deoxy-6-phosphogluconate aldolase
2-keto-3-deoxy-6-phosphogluconic aldolase
-
-
-
-
2-keto-3-deoxygluconate-6-P-aldolase
-
-
-
-
2-keto-3-deoxygluconate-6-phosphate aldolase
-
-
-
-
2-oxo-3-deoxy-6-phosphogluconate aldolase
-
-
-
-
6-phospho-2-dehydro-3-deoxy-D-gluconate D-glyceraldehyde-3-phosphate-lyase
-
-
-
-
6-Phospho-2-keto-3-deoxygluconate aldolase
-
-
-
-
aldolase, phospho-2-keto-3-deoxygluconate
-
-
-
-
KDPG aldolase
KDPG-aldolase
-
-
-
-
ODPG aldolase
-
-
-
-
Phospho-2-dehydro-3-deoxygluconate aldolase
-
-
-
-
Phospho-2-keto-3-deoxygluconate aldolase
-
-
-
-
Phospho-2-keto-3-deoxygluconic aldolase
-
-
-
-
2-keto-3-deoxy-6-phosphogluconate aldolase
-
-
-
-
KDPG aldolase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-dehydro-3-deoxy-6-phospho-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate
mechanism
2-dehydro-3-deoxy-6-phospho-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate
a mechanism is proposed that is based on the crystallographic studies of mutant enzyme E45N
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
condensation
condensation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
2-dehydro-3-deoxy-6-phosphate-D-gluconate D-glyceraldehyde-3-phosphate-lyase (pyruvate-forming)
The enzyme shows no activity with 2-dehydro-3-deoxy-6-phosphate-D-galactonate. cf. EC 4.1.2.55, 2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase [2]. Also acts on 2-oxobutanoate [1].
CAS REGISTRY NUMBER
COMMENTARY
9024-53-7
-
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
2-dehydro-3-deoxy-6-phospho-D-gluconate
pyruvate + D-glyceraldehyde 3-phosphate
-
-
-
?
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
formation of Schiff base intermediate
-
r
2-oxobutyrate + 2-pyridine carboxaldehyde
?
weak substrate for wild-type enzyme, good substrate for K133Q/T161K mutant
-
?
3-fluoropyruvate + 2-pyridine carboxaldehyde
?
weak substrate for wild-type enzyme, good substrate for K133Q/T161K mutant
-
?
pyruvate + D-glyceraldehyde
2-dehydro-3-deoxy-D-gluconate
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
2-dehydro-3-deoxy-6-phospho-D-gluconate
-
-
-
?
2-dehydro-3-deoxy-6-phospho-D-gluconate
pyruvate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
2-dehydro-3-deoxy-D-galactonate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
D-2-dehydro-3-deoxygluconate
pyruvate + D-glyceraldehyde
-
poor substrate
-
?
pyruvate + 2-pyridine carboxaldehyde
?
-
wild-type, 25% of activity with D-glyceraldehyde 3-phosphate, mutant T161S/S184L, 89% of wild-type activity with D-glyceraldehyde 3-phosphate
-
-
r
pyruvate + 3-pyridine carboxaldehyde
?
-
wild-type, 0.5% of activity with D-glyceraldehyde 3-phosphate, mutant T161S/S184L, 1% of wild-type activity with D-glyceraldehyde 3-phosphate
-
-
r
pyruvate + 4-pyridine carboxaldehyde
?
-
wild-type, 3% of activity with D-glyceraldehyde 3-phosphate, mutant T161S/S184L, 2.5% of wild-type activity with D-glyceraldehyde 3-phosphate
-
-
r
pyruvate + D-glyceraldehyde
2-dehydro-3-deoxy-D-gluconate
-
wild-type, 4% of activity with D-glyceraldehyde 3-phosphate, mutant T161S/S184L, 1% of wild-type activity with D-glyceraldehyde 3-phosphate
-
-
r
Pyruvate + D-glyceraldehyde 3-phosphate
6-Phospho-2-dehydro-3-deoxy-D-gluconate
-
mutant T161S/S184L, 15% of wild-type activity
-
-
r
pyruvate + DL-glyceraldehyde 3-phosphate
2-dehydro-3-deoxy-D-gluconate
-
-
-
?
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
-
-
-
-
?
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
-
-
-
r
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
-
-
-
r
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
-
key enzyme in Entner-Doudoroff pathway
-
r
additional information
?
-
-
2-dehydro-3-deoxy-D-galactonate 6-phosphate is a weak substrate
-
-
?
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
2-dehydro-3-deoxy-6-phospho-D-gluconate
pyruvate + D-glyceraldehyde 3-phosphate
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
2-dehydro-3-deoxy-6-phospho-D-gluconate
-
-
-
?
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
-
-
-
-
r
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
-
key enzyme in Entner-Doudoroff pathway
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.6
(4S)-2-oxo-4-hydroxy-4-(2'-pyridyl)butanoate
-
mutant T161S/S18L, pH 7.5, 25°C
3.5
(4S)-2-oxo-4-hydroxy-4-(2'-pyridyl)butanoate
-
mutant T161S/S184F, pH 7.5, 25°C
5.7
(4S)-2-oxo-4-hydroxy-4-(2'-pyridyl)butanoate
-
mutant S184F, pH 7.5, 25°C
43
(4S)-2-oxo-4-hydroxy-4-(2'-pyridyl)butanoate
-
mutant T161S, pH 7.5, 25°C
0.24
2-dehydro-3-deoxy-6-phospho-D-gluconate
-
mutant T161S/S18L, pH 7.5, 25°C
0.69
2-dehydro-3-deoxy-6-phospho-D-gluconate
-
mutant T161S/S184F, pH 7.5, 25°C
1.5
2-dehydro-3-deoxy-D-gluconate
-
mutant enzyme S184L, in 100 mM HEPES, pH 7.5
1.8
2-dehydro-3-deoxy-D-gluconate
-
mutant enzyme S184D, in 100 mM HEPES, pH 7.5
1.9
2-dehydro-3-deoxy-D-gluconate
-
wild type enzyme, in 100 mM HEPES, pH 7.5
2.3
2-dehydro-3-deoxy-D-gluconate
-
mutant enzyme S184A, in 100 mM HEPES, pH 7.5
0.006
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
KA3-L1 variant, pH 7.5, 25°C
0.1
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
wild type enzyme, in 100 mM HEPES, pH 7.5
0.1
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
wild type enzyme, in 20 mM HEPES, pH 7.5, at 23°C
0.15
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
KA1-2 variant, pH 7.5, 25°C
0.16
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
mutant enzyme S184A, in 100 mM HEPES, pH 7.5
0.2
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
mutant enzyme T161A, in 20 mM HEPES, pH 7.5, at 23°C
0.21
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
KA1-3 variant, pH 7.5, 25°C
0.3
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
mutant enzyme T161V, in 20 mM HEPES, pH 7.5, at 23°C
0.35
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
wild-type enzyme, pH 7.5, 25°C
0.35
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
mutant enzyme S184L, in 100 mM HEPES, pH 7.5
0.46
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
KA3-L2 variant, pH 7.5, 25°C
0.95
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
mutant enzyme S184L, in 100 mM HEPES, pH 7.5
1.2
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
mutant enzyme S184D, in 100 mM HEPES, pH 7.5
3
2-dehydro-4-hydroxy-4-(2'-pyridyl)butyrate
-
mutant enzyme S184A, in 100 mM HEPES, pH 7.5
3
2-dehydro-4-hydroxy-4-(2'-pyridyl)butyrate
-
mutant enzyme S184D, in 100 mM HEPES, pH 7.5
3
2-dehydro-4-hydroxy-4-(2'-pyridyl)butyrate
-
mutant enzyme S184L, in 100 mM HEPES, pH 7.5
32
2-dehydro-4-hydroxy-4-(2'-pyridyl)butyrate
-
wild type enzyme, in 100 mM HEPES, pH 7.5
26
2-dehydro-4-hydroxyoctonate
-
mutant enzyme S184L, in 100 mM HEPES, pH 7.5
51
2-dehydro-4-hydroxyoctonate
-
mutant enzyme S184D, in 100 mM HEPES, pH 7.5
56
2-dehydro-4-hydroxyoctonate
-
mutant enzyme S184A, in 100 mM HEPES, pH 7.5
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
19
(4S)-2-oxo-4-hydroxy-4-(2'-pyridyl)butanoate
-
mutant S184F, pH 7.5, 25°C
175
(4S)-2-oxo-4-hydroxy-4-(2'-pyridyl)butanoate
-
mutant T161S, pH 7.5, 25°C
212
(4S)-2-oxo-4-hydroxy-4-(2'-pyridyl)butanoate
-
mutant T161S/S184F, pH 7.5, 25°C
240
(4S)-2-oxo-4-hydroxy-4-(2'-pyridyl)butanoate
-
mutant T161S/S18L, pH 7.5, 25°C
31
2-dehydro-3-deoxy-6-phospho-D-gluconate
-
mutant T161S/S184F, pH 7.5, 25°C
41
2-dehydro-3-deoxy-6-phospho-D-gluconate
-
mutant T161S/S18L, pH 7.5, 25°C
0.019
2-dehydro-3-deoxy-D-gluconate
-
wild type enzyme, in 100 mM HEPES, pH 7.5
0.04
2-dehydro-3-deoxy-D-gluconate
-
mutant enzyme S184A, in 100 mM HEPES, pH 7.5
0.08
2-dehydro-3-deoxy-D-gluconate
-
mutant enzyme S184L, in 100 mM HEPES, pH 7.5
0.11
2-dehydro-3-deoxy-D-gluconate
-
mutant enzyme S184D, in 100 mM HEPES, pH 7.5
0.00029
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
mutant enzyme S184D, in 100 mM HEPES, pH 7.5
0.0026
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
mutant enzyme S184L, in 100 mM HEPES, pH 7.5
0.0063
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
wild type enzyme, in 100 mM HEPES, pH 7.5
0.02
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
mutant enzyme T161V, in 20 mM HEPES, pH 7.5, at 23°C
3.2
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
mutant enzyme S184D, in 100 mM HEPES, pH 7.5
7.8
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
KA3-L1 variant, pH 7.5, 25°C
9.8
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
mutant enzyme T161A, in 20 mM HEPES, pH 7.5, at 23°C
11.2
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
KA3-L2 variant, pH 7.5, 25°C
74
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
mutant enzyme S184L, in 100 mM HEPES, pH 7.5
80
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
wild type enzyme, in 20 mM HEPES, pH 7.5, at 23°C
83
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
wild type enzyme, in 100 mM HEPES, pH 7.5
97
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
mutant enzyme S184A, in 100 mM HEPES, pH 7.5
284
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
wild-type enzyme, pH 7.5, 25°C
6
2-dehydro-4-hydroxy-4-(2'-pyridyl)butyrate
-
mutant enzyme S184D, in 100 mM HEPES, pH 7.5
11
2-dehydro-4-hydroxy-4-(2'-pyridyl)butyrate
-
wild type enzyme, in 100 mM HEPES, pH 7.5
27
2-dehydro-4-hydroxy-4-(2'-pyridyl)butyrate
-
mutant enzyme S184A, in 100 mM HEPES, pH 7.5
40
2-dehydro-4-hydroxy-4-(2'-pyridyl)butyrate
-
mutant enzyme S184L, in 100 mM HEPES, pH 7.5
1.8
2-dehydro-4-hydroxyoctonate
-
mutant enzyme S184D, in 100 mM HEPES, pH 7.5
2.6
2-dehydro-4-hydroxyoctonate
-
mutant enzyme S184A, in 100 mM HEPES, pH 7.5
2.9
2-dehydro-4-hydroxyoctonate
-
mutant enzyme S184L, in 100 mM HEPES, pH 7.5
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.3
(4S)-2-oxo-4-hydroxy-4-(2'-pyridyl)butanoate
-
mutant S184F, pH 7.5, 25°C
4.1
(4S)-2-oxo-4-hydroxy-4-(2'-pyridyl)butanoate
-
mutant T161S, pH 7.5, 25°C
61
(4S)-2-oxo-4-hydroxy-4-(2'-pyridyl)butanoate
-
mutant T161S/S184F, pH 7.5, 25°C
150
(4S)-2-oxo-4-hydroxy-4-(2'-pyridyl)butanoate
-
mutant T161S/S18L, pH 7.5, 25°C
45
2-dehydro-3-deoxy-6-phospho-D-gluconate
-
mutant T161S/S184F, pH 7.5, 25°C
170
2-dehydro-3-deoxy-6-phospho-D-gluconate
-
mutant T161S/S18L, pH 7.5, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S184A
-
the mutation decreases the efficiency of KDPG retro-aldol cleavage only modestly
S184F
-
active site mutation, enhances the substrate specificity to include catalysis of retro-aldol cleavage of (4S)-2-keto-4-hydroxy-4-(2'-pyridyl)butanoate
S184L
-
the mutation is located in the substrate-binding pocket, interacts with the phosphate moiety of KDPG, and improves the catalytic efficiency for the synthesis of a precursor for nikkomycin by 40fold
T161S
-
active site mutation, enhances the substrate specificity to include catalysis of retro-aldol cleavage of (4S)-2-keto-4-hydroxy-4-(2'-pyridyl)butanoate
T161S/S184F
-
active site mutation, working additively to enhance the substrate specificity to include catalysis of retro-aldol cleavage of (4S)-2-keto-4-hydroxy-4-(2'-pyridyl)butanoate
T161S/S184L
-
active site mutation, working additively to enhance the substrate specificity to include catalysis of retro-aldol cleavage of (4S)-2-keto-4-hydroxy-4-(2'-pyridyl)butanoate. Mutations improve the value of kcat/KM (4S)-2-keto-4-hydroxy-4-(2'-pyridyl)butanoate by more than 450fold, resulting in a catalytic efficiency that is comparable to that of the wild-type enzyme with the natural substrate while retaining high stereoselectivity
T84A/I92F/V118A/G141S/T105I
-
KA3-L2 variant, slightly less stable than wild-type
T84A/I92F/V118A/T161A
-
KA3-L1 variant, enhanced activity towards negatively charged glyoxylate and glyceraldehyde-3-phosphate
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, HEPES (100 mM, pH 7.5), NaCl (100 mM), 10% glycerol, at concentrations ranging from 1 to 16 mM, up to 1 year, remains stable
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
Methylophilus methylotrophus AS1 is choosen as a host strain to produce L-lysine from methanol
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shelton, M.C.; Toone, E.J.
Differential dye-ligand chromatography as a general purification protocol for 2-keto-3-deoxy-6-phosphogluconate aldolases
Tetrahedron
6
207-211
1995
Escherichia coli, Pseudomonas putida, Pelomonas saccharophila, Zymomonas mobilis
-
Buchanan, L.V.; Mehta, N.; Pocivavsek, L.; Niranjanakumari, S.; Toone, E.J.; Naismith, J.H.
Initiating a structural study of 2-keto-3-deoxy-6-phosphogluconate aldolase from Escherichia coli
Acta Crystallogr. Sect. D
55
1946-1948
1999
Escherichia coli
Fong, S.; Machajewski, T.D.; Mak, C.C.; Wong, C.
Directed evolution of D-2-keto-3-deoxy-6-phosphogluconate aldolase to new variants for the efficient synthesis of D- and L-sugars
Chem. Biol.
7
873-883
2000
Escherichia coli
Allard, J.; Grochulski, P.; Sygusch, J.
Covalent intermediate trapped in 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase structure at 1.95-A resolution
Proc. Natl. Acad. Sci. USA
98
3679-3684
2001
Escherichia coli (P0A955)
Wymer, N.; Buchanan, L.V.; Henderson, D.; Mehta, N.; Botting, C.H.; Pocivavsek, L.; Fierke, C.A.; Toone, E.J.; Naismith, J.H.
Directed evolution of a new catalytic site in 2-keto-3-deoxy-6-phosphogluconate aldolase from Escherichia coli
Structure
9
1-9
2001
Escherichia coli (P0A955), Escherichia coli
Braga, R.; Hecquet, L.; Blonski, C.
Slow-binding inhibition of 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase
Bioorg. Med. Chem.
12
2965-2972
2004
Escherichia coli
Fullerton, S.W.B.; Griffiths, J.S.; Merkel, A.B.; Cheriyan, M.; Wymer, N.J.; Hutchins, M.J.; Fierke, C.A.; Toone, E.J.; Naismith, J.H.
Mechanism of the class I KDPG aldolase
Bioorg. Med. Chem.
14
3002-3010
2006
Escherichia coli, Thermotoga maritima
Walters, M.J.; Srikannathasan, V.; McEwan, A.R.; Naismith, J.H.; Fierke, C.A.; Toone, E.J.
Characterization and crystal structure of Escherichia coli KDPGal aldolase
Bioorg. Med. Chem.
16
710-720
2008
Escherichia coli
Cheriyan, M.; Toone, E.J.; Fierke, C.A.
Mutagenesis of the phosphate-binding pocket of KDPG aldolase enhances selectivity for hydrophobic substrates
Protein Sci.
16
2368-2377
2007
Escherichia coli
Ishikawa, K.; Gunji, Y.; Yasueda, H.; Asano, K.
Improvement of L-lysine production by Methylophilus methylotrophus from methanol via the Entner-Doudoroff pathway, originating in Escherichia coli
Biosci. Biotechnol. Biochem.
72
2535-2542
2008
Escherichia coli
Cheriyan, M.; Toone, E.J.; Fierke, C.A.
Improving upon nature: active site remodeling produces highly efficient aldolase activity toward hydrophobic electrophilic substrates
Biochemistry
51
1658-1668
2012
Escherichia coli
Schapfl, M.; Baier, S.; Fries, A.; Ferlaino, S.; Waltzer, S.; Mueller, M.; Sprenger, G.A.
Extended substrate range of thiamine diphosphate-dependent MenD enzyme by coupling of two C-C-bonding reactions
Appl. Microbiol. Biotechnol.
102
8359-8372
2018
Escherichia coli (P0A955)
Morita, K.; Nomura, Y.; Ishii, J.; Matsuda, F.; Kondo, A.; Shimizu, H.
Heterologous expression of bacterial phosphoenol pyruvate carboxylase and Entner-Doudoroff pathway in Saccharomyces cerevisiae for improvement of isobutanol production
J. Biosci. Bioeng.
124
263-270
2017
Escherichia coli (P0A955)
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