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Literature summary for 5.3.2.5 extracted from

  • Nakano, T.; Ashida, H.; Mizohata, E.; Matsumura, H.; Yokota, A.
    An evolutionally conserved Lys122 is essential for function in Rhodospirillum rubrum bona fide RuBisCO and Bacillus subtilis RuBisCO-like protein (2010), Biochem. Biophys. Res. Commun., 392, 212-216.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 (DE3) pLysS cells Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
K122E the mutant fails to form a catalytic dimer and does not show any DK-MTP-1-P enolase activity Bacillus subtilis
K122M the mutant fails to form a catalytic dimer and does not show any DK-MTP-1-P enolase activity Bacillus subtilis
K122R the mutant has specific activity of 32% less than that of the wild type enzyme and a lower thermal stability than the wild type enzyme Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.012
-
5-(methylthio)-2,3-dioxopentyl 1-phosphate wild type enzyme, in 50 mM Tris-HCl (pH 8.2), 1 mM MgCl2, at 25°C Bacillus subtilis
0.013
-
5-(methylthio)-2,3-dioxopentyl 1-phosphate mutant enzyme K122R, in 50 mM Tris-HCl (pH 8.2), 1 mM MgCl2, at 25°C Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
His-Bind resin column chromatography and Superose 6 gel filtration Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5-(methylthio)-2,3-dioxopentyl 1-phosphate
-
Bacillus subtilis 2-hydroxy-3-oxo-5-methylthiopentenyl 1-phosphate
-
?

Subunits

Subunits Comment Organism
dimer
-
Bacillus subtilis

Synonyms

Synonyms Comment Organism
DK-MTP-1-P enolase
-
Bacillus subtilis
ribulose-1,5-bisphosphate carboxylase/oxygenase-like protein
-
Bacillus subtilis
RLP
-
Bacillus subtilis
RuBisCO-like protein
-
Bacillus subtilis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
the wild type enzyme shows no decline in activity after incubation at 40°C, and retains about 80% of its original activity after incubation at 45°C Bacillus subtilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
56
-
5-(methylthio)-2,3-dioxopentyl 1-phosphate mutant enzyme K122R, in 50 mM Tris-HCl (pH 8.2), 1 mM MgCl2, at 25°C Bacillus subtilis
83
-
5-(methylthio)-2,3-dioxopentyl 1-phosphate wild type enzyme, in 50 mM Tris-HCl (pH 8.2), 1 mM MgCl2, at 25°C Bacillus subtilis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4400
-
5-(methylthio)-2,3-dioxopentyl 1-phosphate mutant enzyme K122R, in 50 mM Tris-HCl (pH 8.2), 1 mM MgCl2, at 25°C Bacillus subtilis
7100
-
5-(methylthio)-2,3-dioxopentyl 1-phosphate wild type enzyme, in 50 mM Tris-HCl (pH 8.2), 1 mM MgCl2, at 25°C Bacillus subtilis