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Literature summary for 2.7.4.22 extracted from

  • Gagyi, C.; Bucurenci, N.; Sirbu, O.; Labesse, G.; Ionescu, M.; Ofiteru, A.; Assairi, L.; Landais, S.; Danchin, A.; Barzu, O.; Gilles, A.M.
    UMP kinase from the Gram-positive bacterium Bacillus subtilis is strongly dependent on GTP for optimal activity (2003), Eur. J. Biochem., 270, 3196-3204.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
3'-anthraniloyl-2'-deoxyguanosine-5'-triphosphate
-
Bacillus subtilis
dGTP
-
Bacillus subtilis
GTP half-maximum activation is reached at 0.1 mM GTP, in the absence of GTP the enzyme exhibits less than 10% of its maximum activity Bacillus subtilis

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli
expression in Escherichia coli strain BL21(DE3)/pDIA17 Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
UTP
-
Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.008
-
UMP in the absence of GTP Bacillus subtilis
0.03
-
UMP in the presence of GTP Bacillus subtilis
0.05
-
UMP
-
Escherichia coli
0.11
-
5-fluoro-UMP
-
Escherichia coli
0.12
-
5-fluoro-UMP
-
Bacillus subtilis
0.14
-
6-aza-UMP
-
Bacillus subtilis
0.71
-
6-aza-UMP
-
Escherichia coli
0.9
-
ATP
-
Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
26080
-
monomer, calculated from amino acid sequence Bacillus subtilis
26080
-
monomer, mass spectroscopy Bacillus subtilis
28120
-
His-tagged protein, monomer, mass spectroscopy Bacillus subtilis
28250
-
His-tagged protein, monomer, calculated from amino acid sequence Bacillus subtilis
154000
-
gel filtration Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + UMP Escherichia coli
-
ADP + UDP
-
?
ATP + UMP Bacillus subtilis
-
ADP + UDP
-
?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis O31749
-
-
Escherichia coli P0A7E9
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli
-
Bacillus subtilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.6
-
with 6-aza-UMP as substrate Bacillus subtilis
24
-
with 5-fluoro-UMP as substrate Bacillus subtilis
25
-
His-tagged protein Bacillus subtilis
26
-
native protein Bacillus subtilis
67
-
with 6-aza-UMP as substrate Escherichia coli
126
-
with UMP as substrate Escherichia coli
162
-
with 5-fluoro-UMP as substrate Escherichia coli

Storage Stability

Storage Stability Organism
room temperature, 50 mM Tris-HCl (pH 7.4), 0.1 M NaCl, 2 mM UTP, 2 weeks, no loss of activity Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 5-fluoro-UMP
-
Escherichia coli ADP + 5-fluoro-UDP
-
?
ATP + 5-fluoro-UMP
-
Bacillus subtilis ADP + 5-fluoro-UDP
-
?
ATP + 6-aza-UMP
-
Escherichia coli ADP + 6-aza-UDP
-
?
ATP + 6-aza-UMP
-
Bacillus subtilis ADP + 6-aza-UDP
-
?
ATP + UMP
-
Escherichia coli ADP + UDP
-
?
ATP + UMP
-
Bacillus subtilis ADP + UDP
-
?
ATP + UMP pH 7.4, 2 mM MgCl2, 30°C Escherichia coli ADP + UDP
-
?
ATP + UMP pH 7.4, 2 mM MgCl2, 30°C Bacillus subtilis ADP + UDP
-
?

Subunits

Subunits Comment Organism
hexamer alpha6, gel filtration Bacillus subtilis

Synonyms

Synonyms Comment Organism
UMP kinase
-
Escherichia coli
UMP kinase
-
Bacillus subtilis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
42
-
half-maximal inactivation Bacillus subtilis
70
-
half-maximal inactivation in the presence of 1 mM UTP Bacillus subtilis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.022
-
UTP
-
Bacillus subtilis