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 | 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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Rattus norvegicus | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
GlcNAc 2-epimerase | - |
Homo sapiens |
GlcNAc 2-epimerase | - |
Rattus norvegicus |
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 |