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Literature summary for 3.2.2.26 extracted from

  • Hiratsuka, T.; Itoh, N.; Seto, H.; Dairi, T.
    Enzymatic properties of futalosine hydrolase, an enzyme essential to a newly identified menaquinone biosynthetic pathway (2009), Biosci. Biotechnol. Biochem., 73, 1137-1141.
    View publication on PubMed
Search for more literature for 3.2.2.26

Cloned(Commentary)

Cloned (Comment) Organism
expression of maltose-binding protein fusion enzyme in Escherichia coli Thermus thermophilus

Inhibitors

Inhibitors Comment Organism Structure
hypoxanthine product inhibition Thermus thermophilus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.154
-
 futalosine pH 4.5, 80°C Thermus thermophilus

Metals/Ions

Metals/Ions Comment Organism Structure
additional information the enzyme activity is not affected by 1 mM of EDTA, Pb2+, Fe2+, Mg2+, Ba2+, Co2+, Zn2+, Ca2+, Ni2+, Cu2+, and Mn2+ Thermus thermophilus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
23800
-
 4 * 23800, detagged recombinant TTHA0556, SDS-PAGE, 4 * 66300, recombinant MBP-fusion TTHA0556, SDS-PAGE Thermus thermophilus
66300
-
 4 * 23800, detagged recombinant TTHA0556, SDS-PAGE, 4 * 66300, recombinant MBP-fusion TTHA0556, SDS-PAGE Thermus thermophilus
220000
-
 recombinant MBP-fusion TTHA0556, gel filtration Thermus thermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
futalosine + H2O Thermus thermophilus
-
 dehypoxanthine futalosine + hypoxanthine
-
 ?

Organism

Organism UniProt Comment Textmining
Thermus thermophilus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant maltose-binding protein fusion enzyme from Escherichia coli by amylose affinity chromatography and cleavage of the tag by Factor Xa Thermus thermophilus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 recombinant MBP-fusion and detagged enzymes show similar activities Thermus thermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
futalosine + H2O
-
 Thermus thermophilus dehypoxanthine futalosine + hypoxanthine
-
 ?
futalosine + H2O TTHA0556 is absolutely specific for futalosine and shows no no activity with diverse other structurally related nucleotides and nucleosides, overview Thermus thermophilus dehypoxanthine futalosine + hypoxanthine
-
 ?

Subunits

Subunits Comment Organism
homotetramer 4 * 23800, detagged recombinant TTHA0556, SDS-PAGE, 4 * 66300, recombinant MBP-fusion TTHA0556, SDS-PAGE Thermus thermophilus
More quarternary structure, overview Thermus thermophilus

Synonyms

Synonyms Comment Organism
MqnB
-
 Thermus thermophilus
TTHA0556
-
 Thermus thermophilus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
80
-
-
 Thermus thermophilus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.02
-
 futalosine pH 4.5, 80°C Thermus thermophilus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.5
-
-
 Thermus thermophilus

pH Range

pH Minimum pH Maximum Comment Organism
3 9
-
 Thermus thermophilus

Cofactor

Cofactor Comment Organism Structure
additional information no cofactor required Thermus thermophilus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.1
-
 hypoxanthine pH 4.5, 80°C Thermus thermophilus

General Information

General Information Comment Organism
metabolism the enzyme catalyzes the second step of the futalosine pathway starting from chorismate, alternative to the menaquinone pathway, overview Thermus thermophilus