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Literature summary for 2.7.7.23 extracted from

  • Honda, Y.; Nakano, S.; Ito, S.; Dadashipour, M.; Zhang, Z.; Kawarabayasi, Y.
    Improvement of ST0452 N-acetylglucosamine-1-phosphate uridyltransferase activity by the cooperative effect of two single mutations identified through structure-based protein engineering (2018), Appl. Environ. Microbiol., 84, e002213-18 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of mutant enzymes in Escherichia coli Sulfurisphaera tokodaii

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapor diffusion method at 22°C, crystallization of the Y97N protein Sulfurisphaera tokodaii

Protein Variants

Protein Variants Comment Organism
T80S/Y97N the mutant enzyme shows 6.5times-higher activity, compared to that of the wild-type ST0452 protein, revealing that these two substituted residues function cooperatively to increase N-acetylglucosamine-1-phosphate uridyltransferase activity Sulfurisphaera tokodaii
Y97N the mutant enzyme exhibits over 4 times higher N-acetylglucosamine-1-phosphate uridyltransferase activity, compared with that of the wild-type ST0452 protein. The three-dimensional structure of the Y97N protein is not changed by this substitution but the interactions with the substrate are slightly modified, which might cause the activity to increase. The crystal structure of the Y97N protein shows that positions 146 (Glu) and 80 (Thr) form interactions with GlcNAc, and an engineering strategy is applied to these residues to increase activity Sulfurisphaera tokodaii

Organism

Organism UniProt Comment Textmining
Sulfurisphaera tokodaii Q975F9
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Sulfurisphaera tokodaii DSM 16993 Q975F9
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Purification (Commentary)

Purification (Comment) Organism
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Sulfurisphaera tokodaii

Synonyms

Synonyms Comment Organism
ST0452
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Sulfurisphaera tokodaii