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Information on EC 3.2.2.26 - futalosine hydrolase and Organism(s) Thermus thermophilus and UniProt Accession Q5SKT7

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EC Tree
     3 Hydrolases
         3.2 Glycosylases
             3.2.2 Hydrolysing N-glycosyl compounds
                3.2.2.26 futalosine hydrolase
IUBMB Comments
This enzyme, which is specific for futalosine, catalyses the second step of a novel menaquinone biosynthetic pathway that is found in some prokaryotes.
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This record set is specific for:
Thermus thermophilus
UNIPROT: Q5SKT7
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The taxonomic range for the selected organisms is: Thermus thermophilus
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
ttha0556, futalosine hydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
futalosine nucleosidase
-
futalosine hydrolase
-
-
-
-
futalosine nucleosidase
-
-
-
-
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.
SUBSTRATE
PRODUCT                       
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
-
-
-
?
futalosine + H2O
dehypoxanthine futalosine + hypoxanthine
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
futalosine + H2O
dehypoxanthine futalosine + hypoxanthine
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no cofactor required
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the enzyme activity is not affected by 1 mM of EDTA, Pb2+, Fe2+, Mg2+, Ba2+, Co2+, Zn2+, Ca2+, Ni2+, Cu2+, and Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
hypoxanthine
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product inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.154
futalosine
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pH 4.5, 80°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.02
futalosine
-
pH 4.5, 80°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.1
hypoxanthine
-
pH 4.5, 80°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
220000
-
recombinant MBP-fusion TTHA0556, gel filtration
23800
-
4 * 23800, detagged recombinant TTHA0556, SDS-PAGE, 4 * 66300, recombinant MBP-fusion TTHA0556, SDS-PAGE
66300
-
4 * 23800, detagged recombinant TTHA0556, SDS-PAGE, 4 * 66300, recombinant MBP-fusion TTHA0556, SDS-PAGE
SUBUNIT
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
-
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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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of maltose-binding protein fusion enzyme in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hiratsuka, T.; Furihata, K.; Ishikawa, J.; Yamashita, H.; Itoh, N.; Seto, H.; Dairi, T.
An alternative menaquinone biosynthetic pathway operating in microorganisms
Science
321
1670-1673
2008
Streptomyces coelicolor (Q9KXN0), Thermus thermophilus (Q5SKT7), Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q5SKT7)
Manually annotated by BRENDA team
Hiratsuka, T.; Itoh, N.; Seto, H.; Dairi, T.
Enzymatic properties of futalosine hydrolase, an enzyme essential to a newly identified menaquinone biosynthetic pathway
Biosci. Biotechnol. Biochem.
73
1137-1141
2009
Thermus thermophilus
Manually annotated by BRENDA team
Li, X.; Apel, D.; Gaynor, E.C.; Tanner, M.E.
5'-methylthioadenosine nucleosidase is implicated in playing a key role in a modified futalosine pathway for menaquinone biosynthesis in Campylobacter jejuni
J. Biol. Chem.
286
19392-19398
2011
Campylobacter jejuni, Campylobacter jejuni NCTC 11168, Streptomyces coelicolor (Q9KXN0), Thermus thermophilus (Q5SKT7)
Manually annotated by BRENDA team