Information on EC 4.1.2.14 - 2-dehydro-3-deoxy-phosphogluconate aldolase

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

EC NUMBER
COMMENTARY
4.1.2.14
-
RECOMMENDED NAME
GeneOntology No.
2-dehydro-3-deoxy-phosphogluconate aldolase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2-dehydro-3-deoxy-6-phospho-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
2-dehydro-3-deoxy-6-phospho-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
mechanism; Schiff base formation between a lysine epsilon-amino group and carbonyl compounds 6-phospho-2-dehydro-3-deoxy-D-gluconate
-
2-dehydro-3-deoxy-6-phospho-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
stereochemistry, both the exchanging proton from water and D-glyceraldehyde-3-phosphate attack the same face of the enzyme-bound pyruvyleneamine
-
2-dehydro-3-deoxy-6-phospho-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
mechanism
-
2-dehydro-3-deoxy-6-phospho-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
a mechanism is proposed that is based on the crystallographic studies of mutant enzyme E45N
-
2-dehydro-3-deoxy-6-phospho-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
a mechanism is proposed that is based on the crystallographic studies
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
condensation
-
-
-
-
condensation
A4VVI7
-
condensation
-
-
condensation
-
-
condensation
Q704D1, -
-
elimination
A4VVI7
elimination of an aldehyde, C-C bond cleavage
elimination
-
elimination of an aldehyde, C-C bond cleavage
elimination
Q704D1, -
elimination of an aldehyde, C-C bond cleavage
elimination
-
-
of an aldehyde, C-C bond cleavage
-
PATHWAY
KEGG Link
MetaCyc Link
5-dehydro-4-deoxy-D-glucuronate degradation
-
D-fructuronate degradation
-
D-glucosaminate degradation
-
Entner-Doudoroff pathway I
-
Entner-Doudoroff pathway III (semi-phosphorylative)
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
Pentose phosphate pathway
-
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].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2-dehydro-3-deoxyphosphogluconate aldolase
-
-
-
-
2-keto-3-deoxy-(6-phospho)-gluconate aldolase
-
-
2-keto-3-deoxy-(6-phospho)-gluconate aldolase
Q704D1
-
2-keto-3-deoxy-6-phosphogluconate aldolase
-
-
-
-
2-keto-3-deoxy-6-phosphogluconate aldolase
-
-
2-keto-3-deoxy-6-phosphogluconate aldolase
A4VVI7
-
2-keto-3-deoxy-6-phosphogluconate aldolase
-
-
2-keto-3-deoxy-6-phosphogluconate aldolase
-
-
2-keto-3-deoxy-6-phosphogluconate aldolase
Zymomonas mobilis ZM4
-
-
-
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
-
-
-
-
KD(P)G aldolase
-
-
KD(P)G aldolase
Q704D1
-
KDPG aldolase
-
-
-
-
KDPG aldolase
A4VVI7
-
KDPG aldolase
-
-
KDPG aldolase
-
-
KDPG aldolase
Zymomonas mobilis ZM4
-
-
-
KDPG-aldolase
-
-
-
-
ODPG aldolase
-
-
-
-
Phospho-2-dehydro-3-deoxygluconate aldolase
-
-
-
-
Phospho-2-keto-3-deoxygluconate aldolase
-
-
-
-
Phospho-2-keto-3-deoxygluconic aldolase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9024-53-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain Lhet2, strain PW2, strain KLB, strain OP and strain QBP
-
-
Manually annotated by BRENDA team
bifunctional enzyme Ec4.1.2.14/Ec4.1.3.16
-
-
Manually annotated by BRENDA team
strain CC409
-
-
Manually annotated by BRENDA team
Bradyrhizobium japonicum CC409
strain CC409
-
-
Manually annotated by BRENDA team
strain H16
-
-
Manually annotated by BRENDA team
a L-lysine producer of Methylophilus methylotrophus is constructed by the introduction of the Escherichia coli edd-eda operon
-
-
Manually annotated by BRENDA team
strain NZP2213
-
-
Manually annotated by BRENDA team
Mesorhizobium loti NZP2213
strain NZP2213
-
-
Manually annotated by BRENDA team
strain A 3.12
-
-
Manually annotated by BRENDA team
Pelomonas saccharophila A 3.12
strain A 3.12
-
-
Manually annotated by BRENDA team
strain CC224; strain SU391
-
-
Manually annotated by BRENDA team
Rhizobium leguminosarum CC224
strain CC224
-
-
Manually annotated by BRENDA team
Rhizobium leguminosarum SU391
strain SU391
-
-
Manually annotated by BRENDA team
strain RL3001
-
-
Manually annotated by BRENDA team
Rhizobium lupini RL3001
strain RL3001
-
-
Manually annotated by BRENDA team
strain CC365
-
-
Manually annotated by BRENDA team
Rhizobium phaseoli CC365
strain CC365
-
-
Manually annotated by BRENDA team
strain SU216
-
-
Manually annotated by BRENDA team
Sinorhizobium meliloti SU216
strain SU216
-
-
Manually annotated by BRENDA team
serotype 2
UniProt
Manually annotated by BRENDA team
strain ZM4
-
-
Manually annotated by BRENDA team
Zymomonas mobilis ZM4
strain ZM4
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
the eda gene disrupted mutant exhibits no appreciable change in growth characteristics in vitro, but is defective in multiplication within eukaryotic cells
malfunction
Legionella pneumophila AM511
-
the eda gene disrupted mutant exhibits no appreciable change in growth characteristics in vitro, but is defective in multiplication within eukaryotic cells
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-dehydro-3-deoxy-6-phospho-D-gluconate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
r
2-dehydro-3-deoxy-6-phospho-D-gluconate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
?
2-dehydro-3-deoxy-6-phospho-D-gluconate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Q704D1, -
-
-
-
r
2-dehydro-3-deoxy-D-galactonate
pyruvate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
?
2-dehydro-3-deoxy-D-galactonate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
?
2-dehydro-3-deoxy-D-gluconate
pyruvate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
?
2-dehydro-3-deoxy-D-gluconate
pyruvate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
r
2-dehydro-3-deoxy-D-gluconate
pyruvate + D-glyceraldehyde
show the reaction diagram
Q704D1, -
-
-
-
r
2-dehydro-3-deoxy-D-gluconate
?
show the reaction diagram
-
-
-
-
?
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
?
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
r
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
?
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
?
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
A4VVI7
-
-
-
r
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
cleavage reaction is favoured
-
-
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
highly specific in direction of cleavage
-
-
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
P0A955
formation of Schiff base intermediate
-
r
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
formation of Schiff base intermediate
-
r
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
key enzyme in Entner-Doudoroff pathway
-
r
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Rhizobium leguminosarum SU391
-
-
-
-
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Zymomonas mobilis ZM4
-
-
-
-
?
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Rhizobium sp. BICC610, Rhizobium sp. BICC613, Rhizobium phaseoli CC365, Rhizobium sp. BICC609, Rhizobium lupini RL3001
-
-
-
-
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Legionella pneumophila AM511
-
-
-
-
?
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Sinorhizobium meliloti SU216, Rhizobium sp. BICC614, Rhizobium sp. U8, Bradyrhizobium japonicum CC409, Rhizobium leguminosarum CC224, Mesorhizobium loti NZP2213
-
-
-
-
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Pelomonas saccharophila A 3.12
-
-
-
-
-
2-dehydro-4-hydroxy-4-(2'-pyridyl)butyrate
?
show the reaction diagram
-
-
-
-
?
2-dehydro-4-hydroxyoctonate
?
show the reaction diagram
-
-
-
-
?
2-keto-3-deoxy-6-phosphogalactonate
?
show the reaction diagram
-
-
-
-
?
2-oxobutyrate + 2-pyridine carboxaldehyde
?
show the reaction diagram
-
weak substrate for wild-type enzyme, good substrate for K133Q/T161K mutant
-
?
2-oxobutyrate + D-glyceraldehyde
?
show the reaction diagram
-
weak substrate
-
?
2-pyridinecarboxyaldehyde + pyruvate
(S)-4-hydroxy-2-keto-4-(2'-pyridyl)butyrate
show the reaction diagram
-
typical isolated yield of product is 80-90% after reverse-phase C18 purification. Reaction is also doable with substrates other than 2-pyridinecarboxyaldehyde. Enantiomeric excess greater than 99.7%
-
-
?
3-fluoropyruvate + 2-pyridine carboxaldehyde
?
show the reaction diagram
-
weak substrate for wild-type enzyme, good substrate for K133Q/T161K mutant
-
?
3-fluoropyruvate + D-glyceraldehyde
?
show the reaction diagram
-
weak substrate
-
?
pyruvate + 2-pyridine carboxaldehyde
?
show the reaction diagram
-
weak substrate
-
?
pyruvate + benzaldehyde
?
show the reaction diagram
-
-
-
?
pyruvate + D-erythrose
?
show the reaction diagram
-
weak substrate
-
?
pyruvate + D-erythrose
?
show the reaction diagram
-
weak substrate
-
?
Pyruvate + D-erythrose 4-phosphate
3-Deoxy-D-riboheptulosonic acid 7-phosphate
show the reaction diagram
-
28% of the activity with D-glyceraldehyde 3-phosphate
-
-
Pyruvate + D-glyceraldehyde
?
show the reaction diagram
-
35% of the activity with D-glyceraldehyde 3-phosphate
-
-
-
pyruvate + D-glyceraldehyde
2-dehydro-3-deoxy-D-gluconate
show the reaction diagram
-
-
-
?
Pyruvate + D-glyceraldehyde 3-phosphate
6-Phospho-2-dehydro-3-deoxy-D-gluconate
show the reaction diagram
-
-
-
-
-
Pyruvate + D-glyceraldehyde 3-phosphate
6-Phospho-2-dehydro-3-deoxy-D-gluconate
show the reaction diagram
Pelomonas saccharophila, Pelomonas saccharophila A 3.12
-
-
-
-
pyruvate + D-lactaldehyde
?
show the reaction diagram
-
-
-
?
pyruvate + D-threose
?
show the reaction diagram
-
weak substrate
-
?
pyruvate + DL-3-fluoro-2-hydroxypropanal
?
show the reaction diagram
-
-
-
?
pyruvate + DL-glyceraldehyde 3-phosphate
2-dehydro-3-deoxy-D-gluconate
show the reaction diagram
-
-
-
?
pyruvate + glycoaldehyde
?
show the reaction diagram
-
-
-
?
pyruvate + glycoaldehyde
?
show the reaction diagram
-
-
-
?
Pyruvate + glyoxylate
?
show the reaction diagram
-
-
-
?
Pyruvate + glyoxylic acid
?
show the reaction diagram
-
93% of the activity with D-glyceraldehyde 3-phosphate
-
-
-
pyruvate + L-erythrose
?
show the reaction diagram
-
weak substrate
-
?
pyruvate + L-glyceraldehyde 3-phosphate
?
show the reaction diagram
-
weak substrate
-
?
pyruvate + L-threose
?
show the reaction diagram
-
weak substrate
-
?
D-2-dehydro-3-deoxygluconate
pyruvate + D-glyceraldehyde
show the reaction diagram
-
poor substrate
-
?
additional information
?
-
-
catalyzes decarboxylation of oxaloacetate at much slower rate than it cleaves, catalyzes exchange of the methyl hydrogen of pyruvate with protons of water
-
-
-
additional information
?
-
-
catalyzes exchange of the methyl hydrogen of pyruvate with protons of water
-
-
-
additional information
?
-
-
constitutive enzyme
-
-
-
additional information
?
-
-
induced in cells grown on glucose or gluconate
-
-
-
additional information
?
-
-
enzyme of the Entner-Doudoroff pathway
-
-
-
additional information
?
-
-
enzyme of the Entner-Doudoroff pathway
-
-
-
additional information
?
-
-
enzyme of the Entner-Doudoroff pathway
-
-
-
additional information
?
-
-
key enzyme of the Entner-Doudoroff pathway
-
-
-
additional information
?
-
-
key enzyme in Entner-Doudoroff pathway
-
?
additional information
?
-
-
2-dehydro-3-deoxy-D-galactonate 6-phosphate is a weak substrate
-
-
-
additional information
?
-
Rhizobium leguminosarum SU391, Rhizobium sp. BICC610, Rhizobium sp. BICC613, Rhizobium phaseoli CC365, Rhizobium sp. BICC609, Rhizobium lupini RL3001, Sinorhizobium meliloti SU216, Rhizobium sp. BICC614, Rhizobium sp. U8, Bradyrhizobium japonicum CC409, Rhizobium leguminosarum CC224, Mesorhizobium loti NZP2213
-
enzyme of the Entner-Doudoroff pathway
-
-
-
additional information
?
-
Pelomonas saccharophila A 3.12
-
catalyzes exchange of the methyl hydrogen of pyruvate with protons of water
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-dehydro-3-deoxy-6-phospho-D-gluconate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
r
2-dehydro-3-deoxy-6-phospho-D-gluconate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
Q704D1, -
-
-
-
r
2-dehydro-3-deoxy-D-galactonate
pyruvate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
?
2-dehydro-3-deoxy-D-gluconate
pyruvate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
r
2-dehydro-3-deoxy-D-gluconate
pyruvate + D-glyceraldehyde
show the reaction diagram
Q704D1, -
-
-
-
r
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
-
r
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
A4VVI7
-
-
-
r
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
key enzyme in Entner-Doudoroff pathway
-
r
2-keto-3-deoxy-6-phosphogalactonate
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
constitutive enzyme
-
-
-
additional information
?
-
-
induced in cells grown on glucose or gluconate
-
-
-
additional information
?
-
-
enzyme of the Entner-Doudoroff pathway
-
-
-
additional information
?
-
-
enzyme of the Entner-Doudoroff pathway
-
-
-
additional information
?
-
-
enzyme of the Entner-Doudoroff pathway
-
-
-
additional information
?
-
-
key enzyme of the Entner-Doudoroff pathway
-
-
-
additional information
?
-
-
key enzyme in Entner-Doudoroff pathway
-
?
additional information
?
-
Rhizobium leguminosarum SU391, Rhizobium sp. BICC610, Rhizobium sp. BICC613, Rhizobium phaseoli CC365, Rhizobium sp. BICC609, Rhizobium lupini RL3001, Sinorhizobium meliloti SU216, Rhizobium sp. BICC614, Rhizobium sp. U8, Bradyrhizobium japonicum CC409, Rhizobium leguminosarum CC224, Mesorhizobium loti NZP2213
-
enzyme of the Entner-Doudoroff pathway
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
activates
Mg2+
-
activates
Mn2+
-
activates
Ni2+
-
activates
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,4-dioxo-4-phenylbutanoic acid
-
-
2,4-dioxo-4-[2-(trifluoromethyl)phenyl]butanoic acid
-
-
2,4-dioxo-4-[3-(trifluoromethyl)phenyl]butanoic acid
-
-
2,4-dioxo-4-[4-(trifluoromethyl)phenyl]butanoic acid
-
-
2-Keto-(3S)-3-bromopyruvate
-
-
2-Keto-3-deoxy-6-phosphogalaconate
-
-
2-keto-3-deoxygluconate
-
-
4-(3-methoxyphenyl)-2,4-dioxobutanoic acid
-
-
4-(4-methoxyphenyl)-2,4-dioxobutanoic acid
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
5-Keto-4-deoxyglucarate
-
-
acetylpyruvic acid
-
-
Bromopyruvate
-
pyruvate and 2-keto-3-deoxy-6-phosphogluconate protect
Dinitrofluorobenzene
-
-
-
iodoacetamide
-
-
KCl
-
100 mM, 67% inhibition
KI
-
100 mM, 93% inhibition
NaBr
-
100 mM, 88% inhibition
NaCl
-
100 mM, 76% inhibition
NaF
-
100 mM, 45% inhibition
NaI
-
100 mM, 93% inhibition
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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, 25C
0.03
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
KA2 variant, pH 7.5, 25C; KA3 variant, pH 7.5, 25C
0.06
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
pH 7.6, 25C
0.1
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
wild type enzyme, in 20 mM HEPES, pH 7.5, at 23C
0.1
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
wild type enzyme, in 100 mM HEPES, pH 7.5
0.15
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
KA1-2 variant, pH 7.5, 25C
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
-
-
0.2
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
mutant enzyme T161A, in 20 mM HEPES, pH 7.5, at 23C
0.21
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
KA1-3 variant, pH 7.5, 25C
0.22
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
pH 7.5, 40C
0.3
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
mutant enzyme T161V, in 20 mM HEPES, pH 7.5, at 23C
0.35
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
wild-type enzyme, pH 7.5, 25C
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, 25C
0.9
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
pH 7.5, 70C
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; mutant enzyme S184D, in 100 mM HEPES, pH 7.5; 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
150
-
2-dehydro-4-hydroxyoctonate
-
wild type enzyme, in 100 mM HEPES, pH 7.5
0.1
-
2-keto-3-deoxy-6-phosphogluconate
-
-
0.038
-
6-phospho-2-dehydro-3-deoxy-D-gluconate
-
-
0.053
-
6-phospho-2-dehydro-3-deoxy-D-gluconate
-
-
0.073
-
6-phospho-2-dehydro-3-deoxy-D-gluconate
-
-
0.1
-
6-phospho-2-dehydro-3-deoxy-D-gluconate
-
-
0.11
-
6-phospho-2-dehydro-3-deoxy-D-gluconate
-
-
0.25
-
6-phospho-2-dehydro-3-deoxy-D-gluconate
-
-
10.5
-
6-phospho-2-dehydro-3-deoxy-D-gluconate
-
-
26.3
-
benzaldehyde
-
pH 7.5, K133Q/T161K mutant
2
-
D-2-dehydro-deoxygluconate
-
KA3-L1 variant, pH 7.5, 25C
12
-
D-2-dehydro-deoxygluconate
-
KA3-L2 variant, pH 7.5, 25C
13
-
D-2-dehydro-deoxygluconate
-
KA3 variant, pH 7.5, 25C
14
-
D-2-dehydro-deoxygluconate
-
KA2 variant, pH 7.5, 25C
25
-
D-2-dehydro-deoxygluconate
-
KA1-2 variant, pH 7.5, 25C
49
-
D-2-dehydro-deoxygluconate
-
KA1-3 variant, pH 7.5, 25C
55
-
D-2-dehydro-deoxygluconate
-
KA1-4 variant, pH 7.5, 25C
65
-
D-2-dehydro-deoxygluconate
-
KA1-1 variant, pH 7.5, 25C
285
-
D-2-dehydro-deoxygluconate
-
wild-type enzyme, pH 7.5, 25C
10
-
pyruvate
-
pH 7.5, wild-type and K133Q/T161K mutant
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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 23C
0.0333
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
-
2
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
pH 7.5, 40C
2.5
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
KA3 variant, pH 7.5, 25C
3.2
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
mutant enzyme S184D, in 100 mM HEPES, pH 7.5
3.9
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
pH 7.5, 70C
7.8
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
KA3-L1 variant, pH 7.5, 25C
9.8
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
mutant enzyme T161A, in 20 mM HEPES, pH 7.5, at 23C
11.2
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
KA3-L2 variant, pH 7.5, 25C
52
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
KA2 variant, pH 7.5, 25C
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 23C
83
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
wild type enzyme, in 100 mM HEPES, pH 7.5
93
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
KA1-2 variant, pH 7.5, 25C
97
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
mutant enzyme S184A, in 100 mM HEPES, pH 7.5
108
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
KA1-3 variant, pH 7.5, 25C
284
-
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
wild-type enzyme, pH 7.5, 25C
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
-
2-dehydro-4-hydroxyoctonate
-
wild type enzyme, 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
80
-
2-keto-3-deoxy-6-phosphogluconate
-
-
533
-
6-phospho-2-dehydro-3-deoxy-D-gluconate
-
-
0.000001
-
benzaldehyde
-
pH 7.5, K133Q/T161K mutant
0.016
-
D-2-dehydro-deoxygluconate
-
wild-type enzyme, pH 7.5, 25C
0.021
-
D-2-dehydro-deoxygluconate
-
KA3-L1 variant, pH 7.5, 25C
0.1
-
D-2-dehydro-deoxygluconate
-
KA1-1 variant, pH 7.5, 25C
0.11
-
D-2-dehydro-deoxygluconate
-
KA1-4 variant, pH 7.5, 25C
0.13
-
D-2-dehydro-deoxygluconate
-
KA1-3 variant, pH 7.5, 25C
0.16
-
D-2-dehydro-deoxygluconate
-
KA1-2 variant, pH 7.5, 25C
0.43
-
D-2-dehydro-deoxygluconate
-
KA3-L2 variant, pH 7.5, 25C
0.58
-
D-2-dehydro-deoxygluconate
-
KA2 variant, pH 7.5, 25C
1.09
-
D-2-dehydro-deoxygluconate
-
KA3 variant, pH 7.5, 25C
0.0000046
-
pyruvate
-
pH 7.5, K133Q/T161K mutant
0.0121
-
pyruvate
-
pH 7.5, wild-type
6.08
-
D-2-dehydro-deoxygluconate
-
KA2 variant, pH 7.5, 25C; KA3 variant, pH 7.5, 25C
additional information
-
additional information
-
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.07
-
2,4-dioxo-4-phenylbutanoic acid
-
pH 7.6, 25C
0.04
-
2,4-dioxo-4-[2-(trifluoromethyl)phenyl]butanoic acid
-
pH 7.6, 25C
0.03
-
2,4-dioxo-4-[3-(trifluoromethyl)phenyl]butanoic acid
-
pH 7.6, 25C
0.38
-
2,4-dioxo-4-[4-(trifluoromethyl)phenyl]butanoic acid
-
pH 7.6, 25C
0.075
-
4-(3-methoxyphenyl)-2,4-dioxobutanoic acid
-
pH 7.6, 25C
0.18
-
4-(4-methoxyphenyl)-2,4-dioxobutanoic acid
-
pH 7.6, 25C
0.25
-
acetylpyruvic acid
-
pH 7.6, 25C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
8.7
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Vibrio fischeri (strain ATCC 700601 / ES114)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22920
-
A4VVI7
calculated
23000
-
A4VVI7
determined by SDS-PAGE
33000
-
Q704D1, -
-
60000
-
A4VVI7
determined by gel filtration, trimer
70000
-
-
gel filtration
72000
73300
-
meniscus depletion method, low speed equilibrium sedimentation, disc gel electrophoresis
72000
78000
-
disc gel electrophoresis
72000
-
-
high speed equilibrium sedimentation
86150
-
-
equilibrium sedimentation
87830
-
-
equilibrium sedimentation
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 23942, calculation from amino acid sequence determined by Edman method
?
-
x * 21505, SDS-PAGE
dimer
-
2 * 49500, equilibrium sedimentation after treatment with NaBH4 or guanidine hydrochloride
homotrimer
A4VVI7
-
trimer
-
3 * 24000, equilibrium sedimentation after treatment with guanidine HCl and 2-mercaptoethanol
trimer
-
3 * 24000, SDS-PAGE
trimer
-
3 * 23000-24000, SDS-PAGE
trimer
-
3 * 22000, SDS-PAGE
trimer
-
3 * 24000, SDS-PAGE
trimer
-
crystallization experiments
trimer
-
x-ray crystallography
trimer
Zymomonas mobilis ZM4
-
x-ray crystallography
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging drop vapor diffusion method
-
sitting drop vapor diffusion method
-
microdialysis against sequentially higher concentrations of ammonium sulfate
-
structure at 2.8 A resolution
-
the structure of 2-keto-3-deoxy-6-phosphogluconate aldolase is solved at a resolution of 2.8 A
A4VVI7
enzyme in complex with pyruvate, 2-dehydro-3-deoxy-D-gluconate or 2-dehydro-3-deoxy-D-galactonate, determination of the structural basis for substrate promiscuity
-
the crystal structure of the apoprotein is determined to a resolution of 2.0 A, the structure of the protein covalently linked to pyruvate is determined to 2.2 A
Q704D1, -
hanging drop vapor diffusion method, using 25% (w/v) polyethylene glycol 3350, and 0.1 M bis-tris pH 5.5
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1
-
-
4 h, stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
9
-
-
inactivation above
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
highly stable when frozen in phosphate buffer
-
Mg2+ stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, 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
-
-15C or 4C activity of the crystalline enzyme is stable for months
-
protein can be stored at 4C for up to 6 months without a significant loss in activity.
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Ni2+-charged chelating Sepharose Fast Flow column chromatography
-
using a nickel-affinity and a Superdex 200 column
A4VVI7
purified by using Ni2+ affinity column
-
one-step procedure
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli K-12 cells
-
into the plasmid vector pRStac
-
into the vector pET21a for expression in Escherichia coli BL21DE3 cells
A4VVI7
using the pET expression system
-
using the pET expression system
Q704D1, -
expressed in Escherichia coli
-
His6-tagged KDPG aldolase is cloned in Escherichia coli BL21
-
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E9K/V118A
-
KA1-4 variant, improved cleavage of D-2-dehydro-deoxygluconate
G40A/V188A
-
KA1-1 variant, improved cleavage of D-2-dehydro-deoxygluconate
K133Q
-
no aldolase activity
K133Q/T161K
-
reduced catalytic efficiency
S184A
-
the mutation decreases the efficiency of KDPG retro-aldol cleavage only modestly
S184D
-
the mutation leads to strongly reduced enzymatic activity
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
T161A
-
strongly reduced activity
T161V
-
strongly reduced activity
T84A/I92F
-
KA1-2 variant, improved cleavage of D-2-dehydro-deoxygluconate
T84A/I92F/V118A
-
KA2 variant, improved kcat, Km and thermal stability
T84A/I92F/V118A/E138V
-
KA3 variant, small change of melting temperature
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
V118A
-
KA1-3 variant, improved cleavage of D-2-dehydro-deoxygluconate
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
-
application of a KDPG-aldolase gene-dependent addiction system for enhanced production of cyanophycin in Ralstonia eutropha strain H16
synthesis
-
Methylophilus methylotrophus AS1 is choosen as a host strain to produce L-lysine from methanol
medicine
A4VVI7
2-keto-3-deoxy-6-phosphogluconate aldolase is an attractive target for drug therapy in the case of human Streptococcus suis infections
synthesis
-
stereospecific formation of carbon-carbon bonds is one of the major interests in organic synthetic chemistry, aldolases are part of the most important group of asymmetric C-C-bonding enzymes
synthesis
Q704D1, -
stereospecific formation of carbon-carbon bonds is one of the major interests in organic synthetic chemistry, aldolases are part of the most important group of asymmetric C-C-bonding enzymes