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Information on EC 4.1.2.4 - deoxyribose-phosphate aldolase and Organism(s) Yersinia sp. EA015 and UniProt Accession C0LSK9

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
                4.1.2.4 deoxyribose-phosphate aldolase
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This record set is specific for:
Yersinia sp. EA015
UNIPROT: C0LSK9 not found.
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The taxonomic range for the selected organisms is: Yersinia sp. EA015
The enzyme appears in selected viruses and cellular organisms
Synonyms
tgdpa, deoxyriboaldolase, 2-deoxyribose-5-phosphate aldolase, 2-deoxy-d-ribose-5-phosphate aldolase, deoxyribose-5-phosphate aldolase, deoxyribose-phosphate aldolase, deoxyribose 5-phosphate aldolase, 2-deoxy-d-ribose 5-phosphate aldolase, tgdera, d5rp aldolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
deoxyribose 5-phosphate aldolase
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2-Deoxyribose-5-phosphate aldolase
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-
-
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aldolase, deoxyribo
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CGI-26
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Deoxyriboaldolase
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-
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Deoxyribose-5-phosphate aldolase
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-
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DERA
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-
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DR aldolase
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-
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Phosphodeoxyriboaldolase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aldol condensation
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PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
2-deoxy-D-ribose-5-phosphate acetaldehyde-lyase (D-glyceraldehyde-3-phosphate-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9026-97-5
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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
2-deoxy-D-ribose-5-phosphate
D-glyceraldehyde 3-phosphate + acetaldehyde
show the reaction diagram
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-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
2-deoxy-D-ribose-5-phosphate-producing activity of the enzyme remains even at 300 mM acetaldehyde
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.1
2-deoxy-D-ribose-5-phosphate
in 100 mM Tris-HCl buffer, pH 8.8, 0.3 mM NADH, 10 U alcohol dehydrogenase, 1 mM 2-deoxy-D-ribose-5-phosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
137
2.4fold purified enzyme
56
crude extract
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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?
C0LSK9_9GAMM
223
0
23317
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24800
x * 24800, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 24800, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by Ni-NTA affinity chromatography, 2.4fold, with a yield of 43%
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into a pET302/NT-his expression vector and overexpressed in Escherichia coli BL21 (DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
DERA has the potential to resist high concentrations of acetaldehyde and may serve as an industrial catalyst
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kim, Y.M.; Chang, Y.H.; Choi, N.S.; Kim, Y.; Song, J.J.; Kim, J.S.
Cloning, expression, and characterization of a new deoxyribose 5-phosphate aldolase from Yersinia sp. EA015
Protein Expr. Purif.
68
196-200
2009
Yersinia sp. EA015 (C0LSK9)
Manually annotated by BRENDA team