Information on EC 5.3.1.32 - (4S)-4-hydroxy-5-phosphonooxypentane-2,3-dione isomerase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.3.1.32
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RECOMMENDED NAME
GeneOntology No.
(4S)-4-hydroxy-5-phosphonooxypentane-2,3-dione isomerase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(4S)-4-hydroxy-5-phosphonooxypentane-2,3-dione = 3-hydroxy-5-phosphonooxypentane-2,4-dione
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
autoinducer AI-2 degradation
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SYSTEMATIC NAME
IUBMB Comments
(4S)-4-hydroxy-5-phosphonooxypentane-2,3-dione aldose-ketose-isomerase
The enzyme participates in a degradation pathway of the bacterial quorum-sensing autoinducer molecule AI-2.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(4S)-4-hydroxy-5-phosphonooxypentane-2,3-dione
3-hydroxy-5-phosphonooxypentane-2,4-dione
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
(4S)-4-hydroxy-5-phosphonooxypentane-2,3-dione
3-hydroxy-5-phosphonooxypentane-2,4-dione
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diethyldicarbonate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.8
pH 7.2, 30°C, mutant enzyme H70A
20.4
pH 7.2, 30°C, mutant enzyme N25A
61
pH 7.2, 30°C, wild-type enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals of wild-type enzyme with the His6 tag removed are grown via the sitting drop method with a well solution of 1.65 M sodium citrate, pH 6.5. Crystals are cryoprotected in paratone and flash-frozen in the diffractometer cryostream
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli as an N-terminal His6-tagged fusion protein
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E54A
no activity
H65A
no activity
H70A
specific activity is about 1% compared to wild-type activity
N25A
specific activity is about 35% compared to wild-type activity
E54A
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no activity
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H65A
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no activity
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H70A
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specific activity is about 1% compared to wild-type activity
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N25A
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specific activity is about 35% compared to wild-type activity
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Show AA Sequence (511 entries)
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