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Literature summary for 5.1.3.8 extracted from

  • Takahashi, S.; Takahashi, K.; Kaneko, T.; Ogasawara, H.; Shindo, S.; Saito, K.; Kawamura, Y.
    Identification of functionally important cysteine residues of the human renin-binding protein as the enzyme N-acetyl-D-glucosamine 2-epimerase (2001), J. Biochem., 129, 529-535.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
construction of several C-terminal deletion and multi-cysteine/serine mutants and expression in Escherichia coli Homo sapiens

Protein Variants

Protein Variants Comment Organism
C125S no loss of activity compared to wild-type enzyme Homo sapiens
C125S/C210S mutant enzyme shows 54.8% of the activity relative to the wild-type enzyme Homo sapiens
C125S/C210S/C239S mutant enzyme shows 49.3% of the activity relative to the wild-type enzyme Homo sapiens
C125S/C210S/C239S/C203S mutant enzyme shows 28.7% of the activity relative to the wild-type enzyme Homo sapiens
C125S/C210S/C239S/C203S/C386S mutant enzyme shows 23.8% of the activity relative to the wild-type enzyme Homo sapiens
C125S/C210S/C302S/C390S no activity detected Homo sapiens
C125S/C386S mutant enzyme shows 68.7% of the activity relative to the wild-type enzyme Homo sapiens
C125S/C390S mutant enzyme shows 5.1% of the activity relative to the wild-type enzyme Homo sapiens
C210S/C386S mutant enzyme shows 88.7% of the activity relative to the wild-type enzyme Homo sapiens
C210S/C390S mutant enzyme shows 30.9% of the activity relative to the wild-type enzyme Homo sapiens
C239S/C386S mutant enzyme shows 116% of the activity relative to the wild-type enzyme Homo sapiens
C239S/C390S mutant enzyme shows 27.8% of the activity relative to the wild-type enzyme Homo sapiens
C302S/C386S mutant enzyme shows 65.8% of the activity relative to the wild-type enzyme Homo sapiens
C302S/C390S mutant enzyme shows 7.4% of the activity relative to the wild-type enzyme Homo sapiens
C386S no loss of activity compared to wild-type enzyme Homo sapiens
C390S no loss of activity compared to wild-type enzyme Homo sapiens
C41S no loss of activity compared to wild-type enzyme Homo sapiens
C41S/C125S mutant enzyme shows 17.7% of the activity relative to the wild-type enzyme Homo sapiens
C41S/C125S/C210S mutant enzyme shows 28.1% of the activity relative to the wild-type enzyme Homo sapiens
C41S/C125S/C210S/C239S mutant enzyme shows 9.7% of the activity relative to the wild-type enzyme Homo sapiens
C41S/C125S/C210S/C239S/C302S no activity detected Homo sapiens
C41S/C125S/C210S/C239S/C302S/C386S no activity detected Homo sapiens
C41S/C125S/C210S/C239S/C302S/C390S no activity detected Homo sapiens
C41S/C386S mutant enzyme shows 0.7% of the activity relative to the wild-type enzyme Homo sapiens
C41S/C390S no activity detected Homo sapiens
C66S no loss of activity compared to wild-type enzyme Homo sapiens
C66S/C125S mutant enzyme shows 39.4% of the activity relative to the wild-type enzyme Homo sapiens
C66S/C125S/C210S mutant enzyme shows 23.9% of the activity relative to the wild-type enzyme Homo sapiens
C66S/C125S/C210S/C239S mutant enzyme shows 58.4% of the activity relative to the wild-type enzyme Homo sapiens
C66S/C125S/C210S/C239S/C302S mutant enzyme shows 15.5% of the activity relative to the wild-type enzyme Homo sapiens
C66S/C125S/C210S/C302S/C386S no activity detected Homo sapiens
C66S/C125S/C210S/C302S/C390S no activity detected Homo sapiens
C66S/C386S mutant enzyme shows 113% of the activity relative to the wild-type enzyme Homo sapiens
C66S/C390S mutant enzyme shows 14.4% of the activity relative to the wild-type enzyme Homo sapiens
DELTA380-417 mutant enzyme has no activity Homo sapiens
DELTA386-417 mutant enzyme has no activity Homo sapiens
DELTA390-417 mutant enzyme has no activity Homo sapiens
DELTA400-417 C-terminal deletion mutant has approximately 50% activity relative to the wild-type enzyme Homo sapiens
additional information mutational analysis of multi-cysteine/serine mutants reveals that Cys41 and Cys390 are critical for the activity or stabilization of the enzyme, while cysteine residues in the middle of the enzyme, Cys125, Cys210, Cys239, and Cys302 have no essential function in relation to the activity Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
-

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-acetyl-D-mannosamine
-
Homo sapiens N-acetyl-D-glucosamine
-
?