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Literature summary for 5.1.3.8 extracted from

  • Takahashi, S.; Ogasawara, H.; Takahashi, K.; Hori, K.; Saito, K.; Mori, K.
    Identification of a domain conferring nucleotide binding to the N-acetyl-D-glucosamine 2-epimerase (renin binding protein) (2002), J. Biochem., 131, 605-610.
    View publication on PubMed
Search for more literature for 5.1.3.8

Cloned(Commentary)

Cloned (Comment) Organism
construction of a series of chimeric enzymes successively replacing the three domains of the human enzyme - N-terminal, middle, and C-terminal - with the corresponding domains of the rat enzyme. Chimeras are expressed in Escherichia coli JM109 under the control of the Taq promoter Homo sapiens
construction of a series of chimeric enzymes successively replacing the three domains of the human enzyme - N-terminal, middle, and C-terminal - with the corresponding domains of the rat enzyme. Chimeras are expressed in Escherichia coli JM109 under the control of the Taq promoter Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
additional information construction of a series of chimeric enzymes successively replacing the three domains of the human enzyme - N-terminal, middle, and C-terminal - with the corresponding domains of the rat enzyme. Chimerae are expressed in Escherichia coli JM109 under the control of the Taq promoter. Chimeric enzymes of HHR, RHH and RHR - where H is a human type domain and R is a rat type domain - have nearly the same nucleotide specificity as the human enzyme. HRR, HRH, and RRH chimeras have the same nucleotide specificity as the rat enzyme. These results indicate that the middle domain of the enzyme molecule participates in the specificity for and binding of nucleotides Homo sapiens
additional information construction of a series of chimeric enzymes successively replacing the three domains of the human enzyme - N-terminal, middle, and C-terminal - with the corresponding domains of the rat enzyme. Chimeras are expressed in Escherichia coli JM109 under the control of the Taq promoter. Chimeric enzymes of HHR, RHH and RHR - where H is a human type domain and R is a rat type domain - have nearly the same nucleotide specificity as the human enzyme. HRR, HRH, and RRH chimeras have the same nucleotide specificity as the rat enzyme. These results indicate that the middle domain of the enzyme molecule participates in the specificity for and binding of nucleotides Rattus norvegicus

General Stability

General Stability Organism
hydrolysis of wild-type and mutant enzymes by thermolysin in absence of ATP, no hydrolysis in presence of ATP Homo sapiens
hydrolysis of wild-type and mutant enzymes by thermolysin in absence of ATP, no hydrolysis in presence of ATP Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
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Rattus norvegicus
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Synonyms

Synonyms Comment Organism
GlcNAc 2-epimerase
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 Homo sapiens
GlcNAc 2-epimerase
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 Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
ATP required in catalytic amounts, Km: 0.0055 mM Rattus norvegicus
ATP required in catalytic amounts, Km: 0.073 mM Homo sapiens