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Information on EC 2.3.1.245 - 3-hydroxy-5-phosphooxypentane-2,4-dione thiolase and Organism(s) Escherichia coli and UniProt Accession P76143

for references in articles please use BRENDA:EC2.3.1.245
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IUBMB Comments
The enzyme participates in a degradation pathway of the bacterial quorum-sensing autoinducer molecule AI-2.
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This record set is specific for:
Escherichia coli
UNIPROT: P76143
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase, lsrF, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:glycerone phosphate C-acetyltransferase
The enzyme participates in a degradation pathway of the bacterial quorum-sensing autoinducer molecule AI-2.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-hydroxy-5-phosphonooxypentane-2,4-dione + coenzyme A
glycerone phosphate + acetyl-CoA
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-hydroxy-5-phosphonooxypentane-2,4-dione + coenzyme A
glycerone phosphate + acetyl-CoA
show the reaction diagram
the enzyme participates in a degradation pathway of the bacterial quorum-sensing autoinducer molecule AI-2 i.e. (S)-4,5-dihydroxypentane-2,3-dione
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme participates in a degradation pathway of the bacterial quorum-sensing autoinducer molecule AI-2
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decamer
each monomer having an (alphabeta)8-barrel fold, crystalligraphic data
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of the catalytically inactive mutant enzyme K203A
hanging drop method with a well solution of 22% PEG 400, 200 mM MgCl2, 100 mM Tris pH 8.0
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K203A
inactive mutant enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli strain BL21
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Diaz, Z.; Xavier, K.B.; Miller, S.T.
The crystal structure of the Escherichia coli autoinducer-2 processing protein LsrF
PLoS One
4
e6820
2009
Escherichia coli (P76143)
Manually annotated by BRENDA team
Marques, J.C.; Oh, I.K.; Ly, D.C.; Lamosa, P.; Ventura, M.R.; Miller, S.T.; Xavier, K.B.
LsrF, a coenzyme A-dependent thiolase, catalyzes the terminal step in processing the quorum sensing signal autoinducer-2
Proc. Natl. Acad. Sci. USA
111
14235-14240
2014
Escherichia coli (P76143)
Manually annotated by BRENDA team