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Information on EC 4.1.2.21 - 2-dehydro-3-deoxy-6-phosphogalactonate aldolase and Organism(s) Escherichia coli and UniProt Accession Q6BF16

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
                4.1.2.21 2-dehydro-3-deoxy-6-phosphogalactonate aldolase
IUBMB Comments
The enzyme catalyses the last reaction in a D-galactose degradation pathway. cf. EC 4.1.2.55, 2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase.
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This record set is specific for:
Escherichia coli
UNIPROT: Q6BF16
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
kdpgal aldolase, 2-keto-3-deoxy-6-phosphogalactonate aldolase, kdpgal, 6-phospho-2-keto-3-deoxygalactonate aldolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-keto-3-deoxy-6-phosphogalactonate aldolase
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2-dehydro-3-deoxyphosphogalactonate aldolase
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2-keto-3-deoxy-6-phosphogalactonate aldolase
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2-keto-3-deoxy-6-phosphogalactonic aldolase
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2-keto-3-deoxygalactonate-6-phosphate aldolase
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-
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2-oxo-3-deoxy-6-phosphogalactonate aldolase
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2-oxo-3-deoxygalactonate 6-phosphate aldolase
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-
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6-phospho-2-dehydro-3-deoxygalactonate aldolase
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6-Phospho-2-keto-3-deoxygalactonate aldolase
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aldolase, phospho-2-keto-3-deoxygalactonate
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KDPGal aldolase
Phospho-2-keto-3-deoxygalactonic aldolase
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PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
2-dehydro-3-deoxy-6-phospho-D-galactonate D-glyceraldehyde-3-phospho-lyase (pyruvate-forming)
The enzyme catalyses the last reaction in a D-galactose degradation pathway. cf. EC 4.1.2.55, 2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase.
CAS REGISTRY NUMBER
COMMENTARY hide
9030-99-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
pyruvate + D-glyceraldehyde 3-phosphate
2-dehydro-3-deoxy-6-phospho-D-galactonate
show the reaction diagram
-
-
-
?
2-dehydro-3-deoxy-D-galactonate 6-phosphate
?
show the reaction diagram
-
enzyme of the D-galactonate catabolism
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-
?
2-dehydro-3-deoxy-D-galactonate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
pyruvate + D-erythrose 4-phosphate
3-deoxy-D-arabino-heptulosonic acid 7-phosphate
show the reaction diagram
-
-
-
-
r
pyruvate + D-erythrose 4-phosphate
?
show the reaction diagram
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-
-
-
?
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
pyruvate + D-glyceraldehyde 3-phosphate
2-dehydro-3-deoxy-6-phospho-D-galactonate
show the reaction diagram
-
-
-
?
2-dehydro-3-deoxy-D-galactonate 6-phosphate
?
show the reaction diagram
-
enzyme of the D-galactonate catabolism
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-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12 - 0.57
D-erythrose 4-phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.94 - 2.5
D-erythrose 4-phosphate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
V154T
the mutant shows reduced activity compared to the wild type enzyme
F33I/D58N/Q72H/A75V/V85A/V154F
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higher activity compared to the wild type enzyme
additional information
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mutant NR8.276-2 exhibits a 60fold improvement in the ratio kcat/KM relative to that of the wild type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
glutathione-Sepharose 4B resin column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli strain NR7
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Deacon, J.; Cooper, R.A.
D-Galactonate utilisation by enteric bacteria. The catabolic pathway in Escherichia coli
FEBS Lett.
77
201-205
1977
Escherichia coli, Escherichia coli K10, Salmonella enterica subsp. enterica serovar Typhimurium
Manually annotated by BRENDA team
Ran, N.; Draths, K.M.; Frost, J.W.
Creation of a shikimate pathway variant
J. Am. Chem. Soc.
126
6856-6857
2004
Escherichia coli
Manually annotated by BRENDA team
Ran, N.; Frost, J.W.
Directed evolution of 2-keto-3-deoxy-6-phosphogalactonate aldolase to replace 3-deoxy-D-arabino-heptulosonic acid 7-phosphate synthase
J. Am. Chem. Soc.
129
6130-6139
2007
Escherichia coli
Manually annotated by BRENDA team
Bisterfeld, C.; Classen, T.; Kueberl, I.; Henssen, B.; Metz, A.; Gohlke, H.; Pietruszka, J.
Redesigning aldolase stereoselectivity by homologous grafting
PLoS ONE
11
e0156525
2016
Escherichia coli (Q6BF16)
Manually annotated by BRENDA team