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Information on EC 4.1.2.51 - 2-dehydro-3-deoxy-D-gluconate aldolase and Organism(s) Picrophilus torridus and UniProt Accession Q6KZI8

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
                4.1.2.51 2-dehydro-3-deoxy-D-gluconate aldolase
IUBMB Comments
The enzyme from the archaeon Picrophilus torridus is involved in D-glucose and D-galactose catabolism via the nonphosphorylative variant of the Entner-Doudoroff pathway. In the direction of aldol synthesis the enzyme catalyses the formation of 2-dehydro-3-deoxy-D-gluconate and 2-dehydro-3-deoxy-D-galactonate at a similar ratio. It shows no activity with 2-dehydro-3-deoxy-D-gluconate 6-phosphate. cf. EC 4.1.2.14, 2-dehydro-3-deoxy-phosphogluconate aldolase.
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Picrophilus torridus
UNIPROT: Q6KZI8
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The taxonomic range for the selected organisms is: Picrophilus torridus
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
pto1279, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KDG-specific aldolase
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SYSTEMATIC NAME
IUBMB Comments
2-dehydro-3-deoxy-D-gluconate D-glyceraldehyde-3-phosphate-lyase (pyruvate-forming)
The enzyme from the archaeon Picrophilus torridus is involved in D-glucose and D-galactose catabolism via the nonphosphorylative variant of the Entner-Doudoroff pathway. In the direction of aldol synthesis the enzyme catalyses the formation of 2-dehydro-3-deoxy-D-gluconate and 2-dehydro-3-deoxy-D-galactonate at a similar ratio. It shows no activity with 2-dehydro-3-deoxy-D-gluconate 6-phosphate. cf. 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
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
2-dehydro-3-deoxy-D-gluconate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
highly specific for 2-dehydro-3-deoxy-D-gluconate with up to 2000fold-higher catalytic efficiency compared to 2-dehydro-3-deoxy-6-phosphogluconate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-dehydro-3-deoxy-D-gluconate
pyruvate + D-glyceraldehyde
show the reaction diagram
the enzyme from the archaeon Picrophilus torridus is involved in D-glucose and D-galactose catabolism via the nonphosphorylative variant of the Entner-Doudoroff pathway
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3 - 0.4
2-dehydro-3-deoxy-D-gluconate
2.5 - 8
2-dehydro-3-deoxy-D-gluconate 6-phosphate
4.6
D-glyceraldehyde
pH 6.2, 60°C
2.7
pyruvate
pH 6.2, 60°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
24.2 - 26.7
2-dehydro-3-deoxy-D-gluconate
0.34 - 0.36
2-dehydro-3-deoxy-D-gluconate 6-phosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
52 - 89
2-dehydro-3-deoxy-D-gluconate
0.04 - 0.14
2-dehydro-3-deoxy-D-gluconate 6-phosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48
pH 6.2, 60°C, substrate: 2-dehydro-3-deoxy-D-gluconate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 7.5
pH 4.5: 50% of maximal activity, pH 7.5: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme is involved in the nonphosphorylative variant of the Entner–Doudoroff pathway
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120000
gel filtration
32000
4 * 32000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
4 * 32000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
half-life: 20 min
90
half-life: 15 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Reher, M.; Fuhrer, T.; Bott, M.; Schoenheit, P.
The nonphosphorylative Entner-Doudoroff pathway in the thermoacidophilic euryarchaeon Picrophilus torridus involves a novel 2-keto-3-deoxygluconate-specific aldolase
J. Bacteriol.
192
964-974
2010
Picrophilus torridus (Q6KZI8), Picrophilus torridus
Manually annotated by BRENDA team