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

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
4.1.2.21
-
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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aldol addition
condensation
elimination
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
D-galactonate degradation
-
-
Galactose metabolism
-
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L-glucose degradation
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-
Metabolic pathways
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degradation of sugar acids
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Entner Doudoroff pathway
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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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 249-27
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-
Manually annotated by BRENDA team
strain 249-27
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-
Manually annotated by BRENDA team
wild-type strain CB13
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-
Manually annotated by BRENDA team
strain K10
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-
Manually annotated by BRENDA team
Mycobacterium butyricum
-
-
-
Manually annotated by BRENDA team
Mycobacterium jucho
-
-
-
Manually annotated by BRENDA team
strain 279
-
-
Manually annotated by BRENDA team
strain 607
-
-
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
-
-
-
-
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
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
105000
-
gel filtration
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
1 min, stable up to
60
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1 min, about 10% loss of activity
65
-
1 min, about 80% loss of activity
70
-
1 min, complete loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable during isolation and lyophilization
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-78C, 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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