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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) Sulfolobus acidocaldarius and UniProt Accession Q4JC35

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EC Tree
IUBMB 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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Sulfolobus acidocaldarius
UNIPROT: Q4JC35
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Word Map
The taxonomic range for the selected organisms is: Sulfolobus acidocaldarius
The enzyme appears in selected viruses and cellular organisms
Synonyms
2-keto-3-deoxygluconate aldolase, kdg-aldolase, sackdga, kd(p)g-aldolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-keto-3-deoxygluconate aldolase
-
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) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
pyruvate + 2-azidoacetaldehyde
?
show the reaction diagram
-
-
-
?
pyruvate + 3-azido-2-hydroxypropanal
?
show the reaction diagram
-
-
-
?
pyruvate + D-glyceraldehyde
2-dehydro-3-deoxy-D-galactonate
show the reaction diagram
pyruvate + D-glyceraldehyde
2-dehydro-3-deoxy-D-gluconate
show the reaction diagram
pyruvate + D-glyceraldehyde 3-phosphate
2-dehydro-3-deoxy-D-galactonate 6-phosphate
show the reaction diagram
higher activity with D-glyceraldehyde 3-phosphate compared to D-glyceraldehyde
-
-
r
pyruvate + D-glyceraldehyde 3-phosphate
2-dehydro-3-deoxy-D-gluconate 6-phosphate
show the reaction diagram
higher activity with D-glyceraldehyde 3-phosphate compared to D-glyceraldehyde
-
-
r
pyruvate + glycolaldehyde
2-dehydro-3-deoxy-D-xylonate
show the reaction diagram
-
-
-
r
pyruvate + glycolaldehyde
2-dehydro-3-deoxy-L-arabinonate
show the reaction diagram
-
-
-
r
pyruvate + glycolaldehyde
?
show the reaction diagram
-
-
-
?
Pyruvate + glyoxylate
?
show the reaction diagram
-
-
-
r
additional information
?
-
the enzyme shows strict requirement for pyruvate
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.1 - 6.3
D-glyceraldehyde
0.8 - 5.4
pyruvate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.4 - 15.7
D-glyceraldehyde
5.5 - 15
pyruvate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 60
the mutant enzyme V193A is more active than wild-type
50 - 90
50°C: about 65% of maximal activity, 90°C: about 70% of maximal activity, mutant enzyme V193A
60 - 90
60°C: about 50% of maximal activity, 90°C: about 95% of maximal activity, wild-type enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop method, the enzyme crystallizes in two space groups, P3(1)21 and P6(5)22, for which diffraction data are obtained to a maximum resolution of 1.8 and 2.5 A
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
V193A
the mutant enzyme displays a threefold increase in activity compared with wild type enzyme. Increased specific activity at 40–60 °C of this mutant is observed, not only for the condensation of pyruvate with glyceraldehyde, but also for several unnatural acceptor aldehydes. The optimal temperature for activity of SacKdgAV193A is lower than for the wild type enzyme, but enzymatic stability of the mutant is similar to that of the wild type
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90
activity half-life of wild-type enzyme is 100 min, activity half-life of mutant enzyme V193A is 120 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wolterink-van Loo, S.; Siemerink, M.A.; Perrakis, G.; Kaper, T.; Kengen, S.W.; van der Oost, J.
Improving low-temperature activity of Sulfolobus acidocaldarius 2-keto-3-deoxygluconate aldolase
Archaea
2
233-239
2009
Sulfolobus acidocaldarius (Q4JC35), Sulfolobus acidocaldarius
Manually annotated by BRENDA team
Wolterink-van Loo, S.; van Eerde, A.; Siemerink, M.A.; Akerboom, J.; Dijkstra, B.W.; van der Oost, J.
Biochemical and structural exploration of the catalytic capacity of Sulfolobus KDG aldolases
Biochem. J.
403
421-430
2007
Sulfolobus acidocaldarius (Q4JC35), Sulfurisphaera tokodaii (F9VPG1)
Manually annotated by BRENDA team