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Information on EC 4.1.2.55 - 2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase and Organism(s) Saccharolobus solfataricus and UniProt Accession O54288
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4.1.2.55 2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolaseIUBMB Comments
In the archaeon Sulfolobus solfataricus the enzyme is involved in glucose and galactose catabolism via the branched variant of the Entner-Doudoroff pathway. It utilizes 2-dehydro-3-deoxy-6-phosphate-D-gluconate and 2-dehydro-3-deoxy-6-phosphate-D-galactonate with similar catalytic efficiency. In vitro the enzyme can also catalyse the cleavage of the non-phosphorylated forms 2-dehydro-3-deoxy-D-gluconate and 2-dehydro-3-deoxy-D-galactonate with much lower catalytic efficiency. cf. EC 4.1.2.21, 2-dehydro-3-deoxy-6-phosphogalactonate aldolase, and EC 4.1.2.14, 2-dehydro-3-deoxy-phosphogluconate aldolase.
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Word Map
- 4.1.2.55
-
sulfolobus
- solfataricus
-
entner-doudoroff
-
hyperthermophilic
- dehydratase
-
non-phosphorylative
- aldolases
- archaeon
- galactose
- n-acetylneuraminate
-
stereochemical
-
thermoacidophilic
-
nonphosphorylated
-
picrophilus
- acidocaldarius
- dhdps
-
stereoselectivity
- dihydrodipicolinate
- torridus
- synthesis
The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
2-keto-3-deoxygluconate aldolase, kdg-aldolase, sackdga, kd(p)g-aldolase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-dehydro-3-deoxy-6-phospho-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate
(1)
2-dehydro-3-deoxy-6-phospho-D-galactonate = pyruvate + D-glyceraldehyde 3-phosphate
(2)
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
2-dehydro-3-deoxy-6-phosphate-D-gluconate/2-dehydro-3-deoxy-6-phosphate-D-galactonate D-glyceraldehyde-3-phosphate-lyase (pyruvate-forming)
In the archaeon Sulfolobus solfataricus the enzyme is involved in glucose and galactose catabolism via the branched variant of the Entner-Doudoroff pathway. It utilizes 2-dehydro-3-deoxy-6-phosphate-D-gluconate and 2-dehydro-3-deoxy-6-phosphate-D-galactonate with similar catalytic efficiency. In vitro the enzyme can also catalyse the cleavage of the non-phosphorylated forms 2-dehydro-3-deoxy-D-gluconate and 2-dehydro-3-deoxy-D-galactonate with much lower catalytic efficiency. cf. EC 4.1.2.21, 2-dehydro-3-deoxy-6-phosphogalactonate aldolase, and EC 4.1.2.14, 2-dehydro-3-deoxy-phosphogluconate aldolase.
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
preferred substrate
-
-
?
pyruvate + glycolaldehyde
2-dehydro-3-deoxy-D-xylonate
-
-
-
r
pyruvate + glycolaldehyde
2-dehydro-3-deoxy-L-arabinonate
-
-
-
r
2-dehydro-3-deoxy-D-galactonate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
key enzyme in both the non- and the semi-phosphorylative EntnerDoudoroff pathway
-
-
?
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
key enzyme in both the non- and the semi-phosphorylative EntnerDoudoroff pathway
-
-
?
2-dehydro-3-deoxy-L-arabinonate
pyruvate + glycolaldehyde
-
-
-
-
?
pyruvate + D-erythrose
(4S,5S,6R)-4,5,6,7-tetrahydroxy-2-oxoheptanoate
-
formation of (4S,5S,6R)-4,5,6,7-tetrahydroxy-2-oxoheptanoate and (4S,5S,6R)-4,5,6,7-tetrahydroxy-2-oxoheptanoate in the ratio 35:65
-
-
?
pyruvate + D-glyceraldehyde
2-dehydro-3-deoxy-D-galactonate
-
the enzyme exhibits no diastereocontrol for the aldol condensation of its natural substrates pyruvate and D-glyceraldehyde and gives a 50:50 mixture of 2-dehydro-3-deoxy-D-gluconate (anti-(4S,5R)-3-deoxy-2-hexulosonate) and 2-dehydro-3-deoxy-D-galactobate (syn-(4R,5R)-3-deoxy-2-hexulosonate)
-
-
?
pyruvate + D-glyceraldehyde
3-deoxy-D-erythro-hex-2-ulosonate
-
formation of 3-deoxy-D-erythro-hex-2-ulosonate and 3-deoxy-D-threo-hex-2-ulosonate in the ratio 45:55
-
-
?
pyruvate + D-glyceraldehyde
3-deoxy-D-threo-hex-2-ulosonate
-
formation of 3-deoxy-D-erythro-hex-2-ulosonate and 3-deoxy-D-threo-hex-2-ulosonate in the ratio 45:55
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
-
-
r
pyruvate + D-glyceraldehyde acetonide
3-deoxy-5,6-O-(1-methylethylidene)-D-erythro-hex-2-ulosonate
-
highly stereoselective formation of 3-deoxy-5,6-O-(1-methylethylidene)-D-erythro-hex-2-ulosonate in 92% diastereomeric excess
-
-
?
pyruvate + D-threose
(4R,5R,6R)-4,5,6,7-tetrahydroxy-2-oxoheptanoate
-
formation of (4S,5R,6R)-4,5,6,7-tetrahydroxy-2-oxoheptanoate and (4R,5R,6R)-4,5,6,7-tetrahydroxy-2-oxoheptanoate in the ratio 40:60
-
-
?
pyruvate + D-threose
(4S,5R,6R)-4,5,6,7-tetrahydroxy-2-oxoheptanoate
-
formation of (4S,5R,6R)-4,5,6,7-tetrahydroxy-2-oxoheptanoate and (4R,5R,6R)-4,5,6,7-tetrahydroxy-2-oxoheptanoate in the ratio 40:60
-
-
?
pyruvate + L-erythrose
(4R,5R,6S)-4,5,6,7-tetrahydroxy-2-oxoheptanoate
-
formation of (4S,5R,6S)-4,5,6,7-tetrahydroxy-2-oxoheptanoate and (4R,5R,6S)-4,5,6,7-tetrahydroxy-2-oxoheptanoate in the ratio 60:40
-
-
?
pyruvate + L-erythrose
(4S,5R,6S)-4,5,6,7-tetrahydroxy-2-oxoheptanoate
-
formation of (4S,5R,6S)-4,5,6,7-tetrahydroxy-2-oxoheptanoate and (4R,5R,6S)-4,5,6,7-tetrahydroxy-2-oxoheptanoate in the ratio 60:40
-
-
?
pyruvate + L-glyceraldehyde
2-dehydro-3-deoxy-L-galactonate
-
condensation of pyruvate with L-glyceraldehyde proceeds with no stereocontrol, yielding a 53:47 diastereoisomeric mixture of 2-dehydro-3-deoxy-L-gluconate (anti-(4S,5R)-3-deoxy-2-hexulosonate) and 2-dehydro-3-deoxy-L-galactonate (syn-(4S,5S)-3-deoxy-2-hexulosonate)
-
-
?
pyruvate + L-glyceraldehyde
2-dehydro-3-deoxy-L-gluconate
-
condensation of pyruvate with L-glyceraldehyde proceeds with no stereocontrol, yielding a 53:47 diastereoisomeric mixture of 2-dehydro-3-deoxy-L-gluconate (anti-(4S,5R)-3-deoxy-2-hexulosonate) and 2-dehydro-3-deoxy-L-galactonate (syn-(4S,5S)-3-deoxy-2-hexulosonate)
-
-
?
pyruvate + L-glyceraldehyde
3-deoxy-D-erythro-hex-2-ulosonate
-
formation of 3-deoxy-L-threo-hex-2-ulosonate and 3-deoxy-L-erythro-hex-2-ulosonate in the ratio 50:50
-
-
?
pyruvate + L-glyceraldehyde
3-deoxy-D-threo-hex-2-ulosonate
-
formation of 3-deoxy-L-threo-hex-2-ulosonate and 3-deoxy-L-erythro-hex-2-ulosonate in the ratio 50:50
-
-
?
pyruvate + L-glyceraldehyde acetonide
3-deoxy-5,6-O-(1-methylethylidene)-L-threo-hex-2-ulosonate
-
highly stereoselective formation of 3-deoxy-5,6-O-(1-methylethylidene)-L-threo-hex-2-ulosonate in 94% diastereomeric excess
-
-
?
pyruvate + L-threose
(4R,5S,6S)-4,5,6,7-tetrahydroxy-2-oxoheptanoate
-
formation of (4S,5S,6S)-4,5,6,7-tetrahydroxy-2-oxoheptanoate and (4R,5S,6S)-4,5,6,7-tetrahydroxy-2-oxoheptanoate in the ratio 90:10
-
-
?
pyruvate + L-threose
(4S,5S,6S)-4,5,6,7-tetrahydroxy-2-oxoheptanoate
-
formation of (4S,5S,6S)-4,5,6,7-tetrahydroxy-2-oxoheptanoate and (4R,5S,6S)-4,5,6,7-tetrahydroxy-2-oxoheptanoate in the ratio 90:10
-
-
?
additional information
?
-
-
the enzyme displays a relatively broad specificity profile towards nonphosphorylated aldehydes
-
-
?
2-dehydro-3-deoxy-D-galactonate
pyruvate + D-glyceraldehyde
-
-
-
?
2-dehydro-3-deoxy-D-galactonate
pyruvate + D-glyceraldehyde
the same enzyme is responsible for the catabolism of both glucose and galactose
-
-
?
2-dehydro-3-deoxy-D-galactonate
pyruvate + D-glyceraldehyde
catalytic efficiency (kcat/KM) is 295fold lower compared to 2-dehydro-3-deoxy-D-galactonate 6-phosphate
-
-
?
2-dehydro-3-deoxy-D-galactonate
pyruvate + D-glyceraldehyde
lack of stereoselectivity in the condensation reaction of pyruvate and D-glyceraldehyde, forming a mixture of 2-dehydro-3-deoxy-D-gluconate and 2-dehydro-3-deoxy-D-galactonate
-
-
r
2-dehydro-3-deoxy-D-galactonate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
-
-
-
?
2-dehydro-3-deoxy-D-galactonate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
catalytic efficiency (kcat/KM) is 295fold higher compared to 2-dehydro-3-deoxy-D-galactonate
-
-
?
2-dehydro-3-deoxy-D-gluconate
pyruvate + D-glyceraldehyde
-
-
-
?
2-dehydro-3-deoxy-D-gluconate
pyruvate + D-glyceraldehyde
comparison of the catalytic efficiency (kcat/KM) for 2-dehydro-3-deoxy-D-gluconate (1.1 mM/s) and 2-dehydro-3-deoxy-D-gluconate 6-phosphate (643 mM/s) suggests that cleavage of the phosphorylated substrate would be significantly favoured in a situation where both compounds are present. If the 2-dehydro-3-deoxy-D-gluconate kinase is present and active then central metabolism will occur via the part-phosphorylative route.The Km of the kinase for ATP of 2.8 mM is high compared to the likely intracellular concentration, and it is possible that the non-phosphorylative pathway would be favoured under starvation conditions, which could produce pyruvate to allow the citric acid cycle to function without ATP input. regardless of whether Sulfolobus solfataricus uses the part-phosphorylative or the non-phosphorylative Entner-Doudoroff pathway, then the same enzymes can be used for the metabolism of glucose and its C4 epimer galactose
-
-
?
2-dehydro-3-deoxy-D-gluconate
pyruvate + D-glyceraldehyde
the same enzyme is responsible for the catabolism of both glucose and galactose
-
-
?
2-dehydro-3-deoxy-D-gluconate
pyruvate + D-glyceraldehyde
catalytic efficiency (kcat/KM) is 580fold lower compared to 2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
-
?
2-dehydro-3-deoxy-D-gluconate
pyruvate + D-glyceraldehyde
lack of stereoselectivity in the condensation reaction of pyruvate and D-glyceraldehyde, forming a mixture of 2-dehydro-3-deoxy-D-gluconate and 2-dehydro-3-deoxy-D-galactonate
-
-
r
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
catalytic efficiency (kcat/KM) is 580fold higher compared to 2-dehydro-3-deoxy-D-gluconate
-
-
?
2-dehydro-3-deoxy-D-xylonate
pyruvate + glycolaldehyde
non-phosphorylative Entner-Doudoroff pathway for catabolism of D-xylose and L-arabinose
-
-
?
2-dehydro-3-deoxy-D-xylonate
pyruvate + glycolaldehyde
since the substrate is not commercially available a coupled assay is carried out
-
-
r
2-dehydro-3-deoxy-L-arabinonate
pyruvate + glycolaldehyde
non-phosphorylative Entner-Doudoroff pathway for catabolism of D-xylose and L-arabinose
-
-
?
2-dehydro-3-deoxy-L-arabinonate
pyruvate + glycolaldehyde
since the substrate is not commercially available a coupled assay is carried out
-
-
r
pyruvate + D-glyceraldehyde
2-dehydro-3-deoxy-D-galactonate
the enzyme exhibits poor diastereocontrol in many of its aldol reactions, including the reaction of its natural substrates, pyruvate and D-glyceraldehyde, which afford a 55:45 mixture of D-2-keto-3-deoxygluconate and D-2-keto-3-deoxy-galactonate
-
-
r
pyruvate + D-glyceraldehyde
2-dehydro-3-deoxy-D-galactonate
the enzyme shows a lack of facial selectivity, yielding approximately equal quantities of 2-keto-3-deoxy-D-gluconate and 2-keto-3-deoxy-D-galactonate
-
-
r
pyruvate + D-glyceraldehyde
2-dehydro-3-deoxy-D-gluconate
no activity could be detected with D-glyceraldehyde 3-phosphate as substrate in place of glyceraldehyde or with the pyruvate analogues beta-hydroxypyruvate and alpha-ketobutyrate. Studies by other groups reveal activity with D-glyceraldehyde 3-phosphate
-
-
r
pyruvate + D-glyceraldehyde
2-dehydro-3-deoxy-D-gluconate
the enzyme exhibits poor diastereocontrol in many of its aldol reactions, including the reaction of its natural substrates, pyruvate and D-glyceraldehyde, which afford a 55:45 mixture of D-2-keto-3-deoxygluconate and D-2-keto-3-deoxy-galactonate
-
-
r
pyruvate + D-glyceraldehyde
2-dehydro-3-deoxy-D-gluconate
the enzyme shows a lack of facial selectivity, yielding approximately equal quantities of 2-keto-3-deoxy-D-gluconate and 2-keto-3-deoxy-D-galactonate
-
-
r
2-dehydro-3-deoxy-D-galactonate
pyruvate + D-glyceraldehyde
-
-
-
-
?
2-dehydro-3-deoxy-D-galactonate
pyruvate + D-glyceraldehyde
key enzyme in both the non- and the semi-phosphorylative EntnerDoudoroff pathway
-
-
?
2-dehydro-3-deoxy-D-gluconate
pyruvate + D-glyceraldehyde
-
-
-
-
?
2-dehydro-3-deoxy-D-gluconate
pyruvate + D-glyceraldehyde
key enzyme in both the non- and the semi-phosphorylative EntnerDoudoroff pathway
-
-
?
pyruvate + D-glyceraldehyde
2-dehydro-3-deoxy-D-gluconate
-
-
-
r
pyruvate + D-glyceraldehyde
2-dehydro-3-deoxy-D-gluconate
-
the enzyme exhibits no diastereocontrol for the aldol condensation of its natural substrates pyruvate and D-glyceraldehyde and gives a 50:50 mixture of 2-dehydro-3-deoxy-D-gluconate (anti-(4S,5R)-3-deoxy-2-hexulosonate) and 2-dehydro-3-deoxy-D-galactobate (syn-(4R,5R)-3-deoxy-2-hexulosonate)
-
-
?
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
preferred substrate
-
-
?
2-dehydro-3-deoxy-D-galactonate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
-
-
-
?
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
-
-
-
?
2-dehydro-3-deoxy-D-xylonate
pyruvate + glycolaldehyde
non-phosphorylative Entner-Doudoroff pathway for catabolism of D-xylose and L-arabinose
-
-
?
2-dehydro-3-deoxy-L-arabinonate
pyruvate + glycolaldehyde
non-phosphorylative Entner-Doudoroff pathway for catabolism of D-xylose and L-arabinose
-
-
?
2-dehydro-3-deoxy-D-galactonate
pyruvate + D-glyceraldehyde
key enzyme in both the non- and the semi-phosphorylative EntnerDoudoroff pathway
-
-
?
2-dehydro-3-deoxy-D-galactonate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
key enzyme in both the non- and the semi-phosphorylative EntnerDoudoroff pathway
-
-
?
2-dehydro-3-deoxy-D-gluconate
pyruvate + D-glyceraldehyde
key enzyme in both the non- and the semi-phosphorylative EntnerDoudoroff pathway
-
-
?
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
key enzyme in both the non- and the semi-phosphorylative EntnerDoudoroff pathway
-
-
?
2-dehydro-3-deoxy-D-galactonate
pyruvate + D-glyceraldehyde
-
-
-
?
2-dehydro-3-deoxy-D-galactonate
pyruvate + D-glyceraldehyde
the same enzyme is responsible for the catabolism of both glucose and galactose
-
-
?
2-dehydro-3-deoxy-D-gluconate
pyruvate + D-glyceraldehyde
-
-
-
?
2-dehydro-3-deoxy-D-gluconate
pyruvate + D-glyceraldehyde
comparison of the catalytic efficiency (kcat/KM) for 2-dehydro-3-deoxy-D-gluconate (1.1 mM/s) and 2-dehydro-3-deoxy-D-gluconate 6-phosphate (643 mM/s) suggests that cleavage of the phosphorylated substrate would be significantly favoured in a situation where both compounds are present. If the 2-dehydro-3-deoxy-D-gluconate kinase is present and active then central metabolism will occur via the part-phosphorylative route.The Km of the kinase for ATP of 2.8 mM is high compared to the likely intracellular concentration, and it is possible that the non-phosphorylative pathway would be favoured under starvation conditions, which could produce pyruvate to allow the citric acid cycle to function without ATP input. regardless of whether Sulfolobus solfataricus uses the part-phosphorylative or the non-phosphorylative Entner-Doudoroff pathway, then the same enzymes can be used for the metabolism of glucose and its C4 epimer galactose
-
-
?
2-dehydro-3-deoxy-D-gluconate
pyruvate + D-glyceraldehyde
the same enzyme is responsible for the catabolism of both glucose and galactose
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
activity is unaffected by the presence of 0.1 mM ZnCl2
additional information
-
activity is unaffected by the presence of 0.1 mM ZnCl2
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaBH4
69% inactivation in the presence of NaBH% and pyruvate, complete inactivation when the reaction time is increased to 20 min
additional information
no decrease in activity in the presence of 50 mM EDTA
-
additional information
-
no decrease in activity in the presence of 50 mM EDTA
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.17
2-dehydro-3-deoxy-D-galactonate 6-phosphate
60°C, pH not specified in the publication
0.1
2-dehydro-3-deoxy-D-gluconate 6-phosphate
60°C, pH not specified in the publication
9.9
2-dehydro-3-deoxy-D-galactonate
60°C, pH not specified in the publication
25.7
2-dehydro-3-deoxy-D-gluconate
60°C, pH not specified in the publication
5.3
D-glyceraldehyde
70°C, pH is not specified in the publication, wild-type enzyme T157F/Y132V
8
D-glyceraldehyde
70°C, pH is not specified in the publication, mutant enzyme
9.1
D-glyceraldehyde
70°C, pH is not specified in the publication, mutant enzyme T157C/Y132V
1.1
pyruvate
70°C, pH is not specified in the publication, wild-type enzyme
4.1
pyruvate
70°C, pH is not specified in the publication, mutant enzyme T157F/Y132V
39.6
pyruvate
70°C, pH is not specified in the publication, mutant enzyme T157C/Y132V
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
34.8
2-dehydro-3-deoxy-D-galactonate 6-phosphate
60°C, pH not specified in the publication
61.9
2-dehydro-3-deoxy-D-gluconate 6-phosphate
60°C, pH not specified in the publication
6.8
2-dehydro-3-deoxy-D-galactonate
60°C, pH not specified in the publication
28.2
2-dehydro-3-deoxy-D-gluconate
60°C, pH not specified in the publication
0.06
D-glyceraldehyde
70°C, pH is not specified in the publication, mutant enzyme
0.07
D-glyceraldehyde
70°C, pH is not specified in the publication, mutant enzyme T157C/Y132V
5.5
D-glyceraldehyde
70°C, pH is not specified in the publication, wild-type enzyme T157F/Y132V
0.07
pyruvate
70°C, pH is not specified in the publication, mutant enzyme T157C/Y132V
0.075
pyruvate
70°C, pH is not specified in the publication, mutant enzyme T157F/Y132V
4.6
pyruvate
70°C, pH is not specified in the publication, wild-type enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
207
2-dehydro-3-deoxy-D-galactonate 6-phosphate
60°C, pH not specified in the publication
643
2-dehydro-3-deoxy-D-gluconate 6-phosphate
60°C, pH not specified in the publication
0.7
2-dehydro-3-deoxy-D-galactonate
60°C, pH not specified in the publication
1.1
2-dehydro-3-deoxy-D-gluconate
60°C, pH not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
50
-
assay at, 2-dehydro-3-deoxy-D-xylonate and 2-dehydro-3-deoxy-L-arabinonate are less thermally stable than these C6 analogues (2-dehydro-3-deoxy-D-gluconate and 2-dehydro-3-deoxy-D-galactonate), and so their kinetic assays are carried out at 50°C
70
-
assay with 2-dehydro-3-deoxy-D-gluconate or 2-dehydro-3-deoxy-D-galactonate as substrates
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70 - 100
70°C: about 40% of maximal activity, 100°C: about 95% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
comparison of the catalytic efficiency (kcat/KM) for 2-dehydro-3-deoxy-D-gluconate (1.1 mM/s) and 2-dehydro-3-deoxy-D-gluconate 6-phosphate (643 mM/s) suggests that cleavage of the phosphorylated substrate would be significantly favoured in a situation where both compounds are present. If the 2-dehydro-3-deoxy-D-gluconate kinase is present and active then central metabolism will occur via the part-phosphorylative route.The Km of the kinase for ATP of 2.8 mM is high compared to the likely intracellular concentration, and it is possible that the non-phosphorylative pathway would be favoured under starvation conditions, which could produce pyruvate to allow the citric acid cycle to function without ATP input. regardless of whether Sulfolobus solfataricus uses the part-phosphorylative or the non-phosphorylative Entner-Doudoroff pathway, then the same enzymes can be used for the metabolism of glucose and its C4 epimer galactose
physiological function
the enzyme is involved in the non-phosphorylated Entner-Doudoroff pathway of glucose oxidation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop diffusion method, three crystal forms: orthorhombic crystals of space group P2(1)2(1)2(1), which diffract to beyond 2.15 A, monoclinic crystals of space group C2, which diffract to 2.2 A, and cubic crystals of space group P4(2)32, which diffract to 3.4 A
in complex with 2-dehydro-3-deoxy-6-phospho-D-gluconate, vapor diffusion method
trapping of Schiff base complexes with natural substrates pyruvate, 2-dehydro-3-deoxy-D-gluconate, 2-dehydro-3-deoxy-D-galactonate and pyruvate plus D-glyceraldehyde at physiological pH by rapid soaking at low temperature followed by flash freezing prior to X-ray data collection. The complexes explain the substrate promiscuity of the enzyme with a rigid ligand-binding site able to accommodate both 2-dehydro-3-deoxy-D-gluconate and 2-dehydro-3-deoxy-D-galactonate
X-ray crystallographic analysis of the active site of the aldolase bound to pyruvate, 2-dehydro-3-deoxy-D-gluconate and 2-dehydro-3-deoxy-D-galactonate at 4°C, reveals that its catalytic mechanism is typical of the N-acetylneuraminic acid lyase superfamily
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
T157C
improved for 2-dehydro-3-deoxy-D-gluconate with a 75% diastereoisomeric ratio
T157C/Y132V
diastereoselective formation of 2-dehydro-3-deoxy-D-gluconate with much improved (91%) diastereoisomeric ratio
T157F/Y132V
diastereoselective formation of 2-dehydro-3-deoxy-D-gluconate with much improved (93%) diastereoisomeric ratio
T157V/A198L/D181Q
diastereoselective formation of 2-dehydro-3-deoxy-D-galactonate with much improved (88%) diastereoisomeric ratio
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
stereoselectivity is induced into aldol reactions of this naturally promiscuous enzyme by employing D-glyceraldehyde acetonide and L-glyceraldehyde acetonide as substrates
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lamble, H.J.; Heyer, N.I.; Bull, S.D.; Hough, D.W.; Danson, M.J.
Metabolic pathway promiscuity in the archaeon Sulfolobus solfataricus revealed by studies on glucose dehydrogenase and 2-keto-3-deoxygluconate aldolase
J. Biol. Chem.
278
34066-34072
2003
Saccharolobus solfataricus (O54288), Saccharolobus solfataricus
Ahmed, H.; Ettema, T.J.; Tjaden, B.; Geerling, A.C.; van der Oost, J.; Siebers, B.
The semi-phosphorylative Entner-Doudoroff pathway in hyperthermophilic archaea: a re-evaluation
Biochem. J.
390
529-540
2005
Saccharolobus solfataricus (Q97U28), Saccharolobus solfataricus P2 (Q97U28), Thermoproteus tenax
Theodossis, A.; Walden, H.; Westwick, E.J.; Connaris, H.; Lamble, H.J.; Hough, D.W.; Danson, M.J.; Taylor, G.L.
The structural basis for substrate promiscuity in 2-keto-3-deoxygluconate aldolase from the Entner-Doudoroff pathway in Sulfolobus solfataricus
J. Biol. Chem.
279
43886-43892
2004
Saccharolobus solfataricus (O54288), Saccharolobus solfataricus
Hendry, E.J.; Buchanan, C.L.; Russell, R.J.; Hough, D.W.; Reeve, C.D.; Danson, M.J.; Taylor, G.L.
Preliminary crystallographic studies of an extremely thermostable KDG aldolase from Sulfolobus solfataricus
Acta Crystallogr. Sect. D
56
1437-1439
2000
Saccharolobus solfataricus (O54288), Saccharolobus solfataricus
Buchanan, C.L.; Connaris, H.; Danson, M.J.; Reeve, C.D.; Hough, D.W.
An extremely thermostable aldolase from Sulfolobus solfataricus with specificity for non-phosphorylated substrates
Biochem. J.
343
563-570
1999
Saccharolobus solfataricus (O54288), Saccharolobus solfataricus, Saccharolobus solfataricus DSM 1616 (O54288)
Royer, S.F.; Haslett, L.; Crennell, S.J.; Hough, D.W.; Danson, M.J.; Bull, S.D.
Structurally informed site-directed mutagenesis of a stereochemically promiscuous aldolase to afford stereochemically complementary biocatalysts
J. Am. Chem. Soc.
132
11753-11758
2010
Saccharolobus solfataricus (O54288), Saccharolobus solfataricus
Nunn, C.E.; Johnsen, U.; Schoenheit, P.; Fuhrer, T.; Sauer, U.; Hough, D.W.; Danson, M.J.
Metabolism of pentose sugars in the hyperthermophilic archaea Sulfolobus solfataricus and Sulfolobus acidocaldarius
J. Biol. Chem.
285
33701-33709
2010
Saccharolobus solfataricus (O54288), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (O54288)
Lamble, H.J.; Royer, S.F.; Hough, D.W.; Danson, M.J.; Taylor, G.L.; Bull, S.D.
A thermostable aldolase for the synthesis of 3-deoxy-2-ulosonic acids
Adv. Synth. Catal.
349
817-821
2007
Saccharolobus solfataricus
-
Lamble, H.J.; Theodossis, A.; Milburn, C.C.; Taylor, G.L.;, Bull, S.D.; Hough, D.W.; Danson, M.J.
Promiscuity in the part-phosphorylative Entner-Doudoroff pathway of the archaeon Sulfolobus solfataricus
FEBS Lett.
579
6865-6869
2005
Saccharolobus solfataricus (O54288)
Archer, R.M.; Royer, S.F.; Mahy, W.; Winn, C.L.; Danson, M.J.; Bull, S.D.
Syntheses of 2-keto-3-deoxy-D-xylonate and 2-keto-3-deoxy-L-arabinonate as stereochemical probes for demonstrating the metabolic promiscuity of Sulfolobus solfataricus towards D-xylose and L-arabinose
Chemistry
19
2895-2902
2013
Saccharolobus solfataricus
Lamble, H.J.; Danson, M.J.; Hough, D.W.; Bull, S.D.
Engineering stereocontrol into an aldolase-catalysed reaction
Chem. Commun. (Camb. )
2005
124-126
2005
Saccharolobus solfataricus
Zaitsev, V.; Johnsen, U.; Reher, M.; Ortjohann, M.; Taylor, G.L.; Danson, M.J.; Schoenheit, P.; Crennell, S.J.
Insights into the substrate specificity of archaeal Entner-Doudoroff aldolases the structures of Picrophilus torridus 2-keto-3-deoxygluconate aldolase and Sulfolobus solfataricus 2-keto-3-deoxy-6-phosphogluconate aldolase in complex with 2-keto-3-deoxy-6
Biochemistry
57
3797-3806
2018
Saccharolobus solfataricus (O54288), Saccharolobus solfataricus
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