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Literature summary for 2.7.7.9 extracted from

  • Zhang, Z.; Shimizu, Y.; Kawarabayasi, Y.
    Characterization of the amino acid residues mediating the unique amino-sugar-1-phosphate acetyltransferase activity of the archaeal ST0452 protein (2015), Extremophiles, 19, 417-427.
    View publication on PubMed
Search for more literature for 2.7.7.9

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli strain BL21-Codon Plus(DE3)-RIL Sulfurisphaera tokodaii

Protein Variants

Protein Variants Comment Organism
additional information the UTP-glucose-1-phosphate uridylyltransferase activity of mutant enzyme DC005 is reduced by 10%, as compared to that of the wild-type ST0452 protein, while the activity of DC011 is increased by 18%, indicating that the enzymatic activity in the N-terminal region is not greatly affected by truncation of the C-terminal 5 or 11 residues. The mutant enzyme DC011 (deletion of the C-terminal 11 residues of the ST0452 protein) shows little thermal stability at 80°C. The C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein. The deletion mutant enzymes DC021, DC031, DC041, DC071 and DC121, are produced in an insoluble form or aggregated immediately after purification. Mutant enzymes DC051 and DC171 can be expressed in a soluble form. Mutant enzyme DC051 becomes completely insoluble after 5 min treatment at 60°C, while mutant enzyme DC171 is insoluble after 5 min treatment at 70 °C Sulfurisphaera tokodaii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UTP + alpha-D-glucose 1-phosphate Sulfurisphaera tokodaii
-
 diphosphate + UDP-alpha-D-glucose
-
 ?

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
2
-
 pH 7.5, 80°C, mutant enzyme DC05 (deletion of the C-terminal 5 residues of the ST0452 protein) Sulfurisphaera tokodaii
2.2
-
 pH 7.5, 80°C, wild-type enzyme enzyme Sulfurisphaera tokodaii
2.6
-
 pH 7.5, 80°C, mutant enzyme DC011 (deletion of the C-terminal 11 residues of the ST0452 protein) Sulfurisphaera tokodaii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UTP + alpha-D-glucose 1-phosphate
-
 Sulfurisphaera tokodaii diphosphate + UDP-alpha-D-glucose
-
 ?

Subunits

Subunits Comment Organism
trimer the C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form Sulfurisphaera tokodaii

Synonyms

Synonyms Comment Organism
GlcNAc-1-P UTase
-
 Sulfurisphaera tokodaii
ST0452 protein
-
 Sulfurisphaera tokodaii
STK_04520 locus name Sulfurisphaera tokodaii

Temperature Optimum [°C]

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
80
-
 mutant enzyme DC005 shows the same thermostability as wild-type ST0452 protein, whereas mutant enzyme DC011 denatures and becomes insoluble form by 5-min treatment at 80 °C. The C-terminal domain of the ST0452 protein, with its LbetaH structure, appears to be essential for the formation of its trimeric form and, in turn, the high stability of the entire ST0452 protein Sulfurisphaera tokodaii

pH Optimum

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