Information on EC 1.1.1.127 - 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.127
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RECOMMENDED NAME
GeneOntology No.
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-dehydro-3-deoxy-D-gluconate + NAD+ = (4S)-4,6-dihydroxy-2,5-dioxohexanoate + NADH + H+
show the reaction diagram
The enzyme from Pseudomas acts equally well on NAD+ or NADP+, while that from Erwinia chrysanthemi and E. coli is more specific for NAD+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3,6-anhydro-alpha-L-galactopyranose degradation
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4-deoxy-L-threo-hex-4-enopyranuronate degradation
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Pentose and glucuronate interconversions
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SYSTEMATIC NAME
IUBMB Comments
2-dehydro-3-deoxy-D-gluconate:NAD+ 5-oxidoreductase
The enzyme from Pseudomonas acts equally well on NAD+ or NADP+, while that from Erwinia chrysanthemi and Escherichia coli is more specific for NAD+.
CAS REGISTRY NUMBER
COMMENTARY hide
37250-56-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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-D-gluconate + NAD+
(4S)-4,6-dihydroxy-2,5-dioxohexanoate + NADH
show the reaction diagram
pyruvate + NAD+
? + NADH
show the reaction diagram
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10% of the activity compared to 2-dehydro-3-deoxy-D-gluconate
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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-D-gluconate + NAD+
(4S)-4,6-dihydroxy-2,5-dioxohexanoate + NADH
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
NADPH
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62% lower activity than with NADH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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20% activation at 1 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ag+
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72% inhibition at 0.01 mM
ATP
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30% inhibition for both reduction and oxidation reaction at 1 mM
p-chloromercuribenzoate
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50% inhibition at 0.02 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.34
(4S)-4,6-dihydroxy-2,5-dioxohexanoate
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7.7
2-dehydro-3-deoxy-D-gluconate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.5
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reduction reaction
10
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oxidation reaction
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
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stable for 15 h
46
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half-life: 10 min, NADH increases thermal stability
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
1 mM NAD+ or NADP+ increase stability
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 2 mM DTT, 6 months
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0-3°C, 1 mM NAD+ or NADP+, 50-67% retaining activity after 5 weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to homogeneity, 2step chromatography
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Show AA Sequence (465 entries)
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