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Information on EC 4.1.2.4 - deoxyribose-phosphate aldolase and Organism(s) Aeropyrum pernix and UniProt Accession Q9Y948

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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:
Aeropyrum pernix
UNIPROT: Q9Y948 not found.
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Word Map
The taxonomic range for the selected organisms is: Aeropyrum pernix
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, d5rp aldolase, 2-deoxyribose 5-phosphate aldolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-Deoxyribose-5-phosphate aldolase
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-
-
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aldolase, deoxyribo
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-
-
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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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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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-
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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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-
r
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.057
2-deoxy-D-ribose 5-phosphate
50°C, pH 6.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
K1
Uniprot
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24000
4 * 24000, SDS-PAGE
93000
gel-filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
4 * 24000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
no loss of activity after 10 min
80
no loss of activity after 60 min
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ethanol
stable up to 40% for 30 min at 50°C
Methanol
stable up to 50% for 30 min at 50°C
N,N-dimethylformamide
stable up to 50% for 30 min at 50°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressen in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sakuraba, H.; Tsuge, H.; Shimoya, I.; Kawakami, R.; Goda, S.; Kawarabayasi, Y.; Katunuma, N.; Ago, H.; Miyano, M.; Ohshima, T.
The first crystal structure of archaeal aldolase. Unique tetrameric structure of 2-deoxy-D-ribose-5-phosphate aldolase from the hyperthermophilic archaea Aeropyrum pernix
J. Biol. Chem.
278
10799-10806
2003
Aeropyrum pernix (Q9Y948), Aeropyrum pernix
Manually annotated by BRENDA team