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Literature summary for 2.3.1.276 extracted from

  • Zhang, Z.; Akutsu, J.; Kawarabayasi, Y.
    Identification of novel acetyltransferase activity on the thermostable protein ST0452 from Sulfolobus tokodaii strain 7 (2010), J. Bacteriol., 192, 3287-3293.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
Mn2+ 2 mM, 80% inhibition Sulfurisphaera tokodaii
Zn2+ 2 mM, 75% inhibition Sulfurisphaera tokodaii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.63
-
acetyl-CoA pH 7.5, 80°C Sulfurisphaera tokodaii
1.71
-
alpha-D-galactosamine 1-phosphate pH 7.5, 80°C Sulfurisphaera tokodaii

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ 2 mM, enhances galactosamine-1-phosphate N-acetyltransferase activity 2.1fold Sulfurisphaera tokodaii
Co2+ 2 mM, enhances galactosamine-1-phosphate N-acetyltransferase activity 1.2fold Sulfurisphaera tokodaii
Mg2+ 2 mM, enhances galactosamine-1-phosphate N-acetyltransferase activity 1.4fold Sulfurisphaera tokodaii

Organism

Organism UniProt Comment Textmining
Sulfurisphaera tokodaii Q975F9
-
-
Sulfurisphaera tokodaii 7 Q975F9
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Sulfurisphaera tokodaii

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
38.4
-
pH 7.5, 80°C, substrates: acetyl-CoA + alpha-D-galactosamine 1-phosphate Sulfurisphaera tokodaii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + alpha-D-galactosamine 1-phosphate no activity with alpha-D-glucosamine 6-phosphate Sulfurisphaera tokodaii CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
80
-
assay at Sulfurisphaera tokodaii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
69.7
-
alpha-D-galactosamine 1-phosphate pH 7.5, 80°C Sulfurisphaera tokodaii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Sulfurisphaera tokodaii

General Information

General Information Comment Organism
physiological function because the multifunctional ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-alpha-D-glucosamine from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-alpha-D-glucosamine biosynthesis pathway in this archaeon Sulfurisphaera tokodaii

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
40.8
-
alpha-D-galactosamine 1-phosphate pH 7.5, 80°C Sulfurisphaera tokodaii