Information on EC 3.2.2.26 - futalosine hydrolase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.2.2.26
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RECOMMENDED NAME
GeneOntology No.
futalosine hydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
futalosine + H2O = dehypoxanthine futalosine + hypoxanthine
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
1,4-dihydroxy-6-naphthoate biosynthesis I
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Biosynthesis of secondary metabolites
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Ubiquinone and other terpenoid-quinone biosynthesis
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1,4-dihydroxy-6-naphthoate biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
futalosine ribohydrolase
This enzyme, which is specific for futalosine, catalyses the second step of a novel menaquinone biosynthetic pathway that is found in some prokaryotes.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
no activity in Campylobacter jejuni
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Manually annotated by BRENDA team
no activity in Chlamydia trachomatis
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-
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Manually annotated by BRENDA team
no activity in Helicobacter pylori strain 26695
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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the enzyme catalyzes the second step of the futalosine pathway starting from chorismate, alternative to the menaquinone pathway, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
6-amino-6-deoxyfutalosine + H2O
dehypoxanthine futalosine + adenine
show the reaction diagram
aminodeoxyfutalosine + H2O
dehypoxanthine futalosine + adenine
show the reaction diagram
futalosine + H2O
dehypoxanthine futalosine + hypoxanthine
show the reaction diagram
additional information
?
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no activity with aminodeoxyfutalosine
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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
futalosine + H2O
dehypoxanthine futalosine + hypoxanthine
show the reaction diagram
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no cofactor required
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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the enzyme activity is not affected by 1 mM of EDTA, Pb2+, Fe2+, Mg2+, Ba2+, Co2+, Zn2+, Ca2+, Ni2+, Cu2+, and Mn2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
hypoxanthine
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product inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00103
6-amino-6-deoxyfutalosine
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at pH 7.0 and 25C
0.154
futalosine
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pH 4.5, 80C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.53
6-amino-6-deoxyfutalosine
Campylobacter jejuni
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at pH 7.0 and 25C
1.02
futalosine
Thermus thermophilus
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pH 4.5, 80C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.1
hypoxanthine
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pH 4.5, 80C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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recombinant MBP-fusion and detagged enzymes show similar activities
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23800
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4 * 23800, detagged recombinant TTHA0556, SDS-PAGE, 4 * 66300, recombinant MBP-fusion TTHA0556, SDS-PAGE
66300
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4 * 23800, detagged recombinant TTHA0556, SDS-PAGE, 4 * 66300, recombinant MBP-fusion TTHA0556, SDS-PAGE
220000
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recombinant MBP-fusion TTHA0556, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
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4 * 23800, detagged recombinant TTHA0556, SDS-PAGE, 4 * 66300, recombinant MBP-fusion TTHA0556, SDS-PAGE
additional information
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quarternary structure, overview
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant maltose-binding protein fusion enzyme from Escherichia coli by amylose affinity chromatography and cleavage of the tag by Factor Xa
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Sepharose column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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expression of maltose-binding protein fusion enzyme in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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strain lacking the activity accumulates futalosine. Recombinant expression does not result in an active enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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