Information on EC 4.1.2.21 - 2-dehydro-3-deoxy-6-phosphogalactonate aldolase

for references in articles please use BRENDA:EC4.1.2.21
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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
4.1.2.21
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RECOMMENDED NAME
GeneOntology No.
2-dehydro-3-deoxy-6-phosphogalactonate aldolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-dehydro-3-deoxy-6-phospho-D-galactonate = pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aldol addition
condensation
elimination
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
D-galactonate degradation
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L-glucose degradation
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degradation of sugar acids
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Entner Doudoroff pathway
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Galactose metabolism
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Metabolic 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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
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Manually annotated by BRENDA team
wild-type strain CB13
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-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
Mycobacterium butyricum
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-
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Manually annotated by BRENDA team
Mycobacterium jucho
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-
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Manually annotated by BRENDA team
strain L5-30, and mutant strain UR23 lacking the enzyme
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-
Manually annotated by BRENDA team
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-galactonate
pyruvate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
?
2-dehydro-3-deoxy-D-galactonate 6-phosphate
?
show the reaction diagram
2-dehydro-3-deoxy-D-galactonate 6-phosphate
pyruvate + D-glyceraldehyde 3-phosphate
show the reaction diagram
2-dehydro-3-deoxy-D-gluconate
pyruvate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
r
2-keto-3-deoxy-6-phosphogalactonate
?
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
-
-
-
-
?
pyruvate + D-glyceraldehyde 3-phosphate
2-dehydro-3-deoxy-D-galactonate 6-phosphate
show the reaction diagram
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-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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-galactonate
pyruvate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
?
2-dehydro-3-deoxy-D-galactonate 6-phosphate
?
show the reaction diagram
2-dehydro-3-deoxy-D-gluconate
pyruvate + D-glyceraldehyde
show the reaction diagram
-
-
-
-
r
2-keto-3-deoxy-6-phosphogalactonate
?
show the reaction diagram
-
-
-
-
?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Bromopyruvate
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3(R,S)-[3-3H2]bromopyruvate is asymetrically detritiated by the enzyme yielding 3(S)-[3-3H,H]bromopyruvate concomitant with inactivation
PCMB
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0.5 mM, 25% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05 - 0.5
2-dehydro-3-deoxy-D-galactonate 6-phosphate
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 7.8
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7.8
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Tris buffer or phosphate buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3 - 9
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pH 6.3: about 75% of maximal activity, pH 9.0: about 30% of maximal activity
6.5 - 9.5
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more than 50% of maximal activity at pH 6.5 and at pH 9.5
PDB
SCOP
CATH
UNIPROT
ORGANISM
Escherichia coli (strain K12);
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
105000
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gel filtration
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
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1 min, stable up to
60
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1 min, about 10% loss of activity
65
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1 min, about 80% loss of activity
70
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1 min, complete loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable during isolation and lyophilization
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-78°C, stable for at least months
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activity of frozen preparations declines about 20% in 2 weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glutathione-Sepharose 4B resin column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain NR7
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using the pET expression system
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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