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Information on EC 4.1.2.14 - 2-dehydro-3-deoxy-phosphogluconate aldolase and Organism(s) Thermoproteus tenax and UniProt Accession Q704D1

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
                4.1.2.14 2-dehydro-3-deoxy-phosphogluconate aldolase
IUBMB 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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This record set is specific for:
Thermoproteus tenax
UNIPROT: Q704D1
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Word Map
The taxonomic range for the selected organisms is: Thermoproteus tenax
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
2-keto-3-deoxy-6-phosphogluconate aldolase, kdpg aldolase, kdpga, phospho-2-keto-3-deoxygluconate aldolase, kd(p)g aldolase, kdpg-aldolase, 2-dehydro-3-deoxy-phosphogluconate aldolase, 2-dehydro-3-deoxyphosphogluconate aldolase, 2-keto-3-deoxy-(6-phospho)-gluconate aldolase, 6-phospho-2-keto-3-deoxygluconate aldolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-keto-3-deoxy-(6-phospho)-gluconate aldolase
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KD(P)G aldolase
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2-dehydro-3-deoxyphosphogluconate aldolase
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-
-
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2-keto-3-deoxy-6-phosphogluconate aldolase
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-
-
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2-keto-3-deoxy-6-phosphogluconic aldolase
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-
-
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2-keto-3-deoxygluconate-6-P-aldolase
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-
-
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2-keto-3-deoxygluconate-6-phosphate aldolase
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-
-
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2-oxo-3-deoxy-6-phosphogluconate aldolase
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-
-
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6-phospho-2-dehydro-3-deoxy-D-gluconate D-glyceraldehyde-3-phosphate-lyase
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-
-
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6-Phospho-2-keto-3-deoxygluconate aldolase
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-
-
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aldolase, phospho-2-keto-3-deoxygluconate
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-
-
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KDPG aldolase
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-
-
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KDPG-aldolase
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-
-
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ODPG aldolase
-
-
-
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Phospho-2-dehydro-3-deoxygluconate aldolase
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-
-
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Phospho-2-keto-3-deoxygluconate aldolase
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-
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Phospho-2-keto-3-deoxygluconic aldolase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
elimination of an aldehyde, C-C bond cleavage
condensation
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-
-
-
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 hide
9024-53-7
-
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-6-phospho-D-gluconate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
2-dehydro-3-deoxy-D-gluconate
pyruvate + D-glyceraldehyde
show the reaction diagram
-
-
-
r
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-6-phospho-D-gluconate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
r
2-dehydro-3-deoxy-D-gluconate
pyruvate + D-glyceraldehyde
show the reaction diagram
-
-
-
r
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KDGA_THETE
306
0
33287
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
using the pET expression system
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pauluhn, A.; Ahmed, H.; Lorentzen, E.; Buchinger, S.; Schomburg, D.; Siebers, B.; Pohl, E.
Crystal structure and stereochemical studies of KD(P)G aldolase from Thermoproteus tenax
Proteins
72
35-43
2008
Saccharolobus solfataricus, Thermoproteus tenax (Q704D1), Thermoproteus tenax
Manually annotated by BRENDA team