Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant enzymes in Escherichia coli strain JM109 | Micrococcus luteus |
Crystallization (Comment) | Organism |
---|---|
C-terminally truncated enzyme, hanging-drop, vapor-diffusion method at 25°C, X-ray diffraction structure determination and analysis at 2.4 resolution using multiple-wavelength anomalous dispersion, MAD | Micrococcus luteus |
Protein Variants | Comment | Organism |
---|---|---|
K67E | site-directed mutagenesis, catalytic residue mutant, inactiv | Micrococcus luteus |
S64A | site-directed mutagenesis, catalytic residue mutant, inactiv | Micrococcus luteus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
additional information | the enzyme is salt-tolerant, the C-terminally truncated enzyme shows higher salt tolerance than the full-length enzyme, the N-terminal domain has abundant glutamic acid residues on its surface, which may explain its salt-tolerant mechanism | Micrococcus luteus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
42000 | - |
2 * 48000, full-length enzyme, SDS-PAGE, 2 * 42000, C-terminally truncated enzyme, SDS-PAGE | Micrococcus luteus |
48000 | - |
2 * 48000, full-length enzyme, SDS-PAGE, 2 * 42000, C-terminally truncated enzyme, SDS-PAGE | Micrococcus luteus |
86000 | - |
C-terminally truncated enzyme, gel filtration | Micrococcus luteus |
96000 | - |
full-length enzyme, gel filtration | Micrococcus luteus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamine + H2O | Micrococcus luteus | - |
L-glutamate + NH3 | - |
? | |
L-glutamine + H2O | Micrococcus luteus K-3 | - |
L-glutamate + NH3 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Micrococcus luteus | - |
- |
- |
Micrococcus luteus K-3 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant enzymes from Escherichia coli strain JM109 | Micrococcus luteus |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
L-glutamine + H2O = L-glutamate + NH3 | active site structure, the enzyme contains a catalytic dyad formed by S64 and K67 | Micrococcus luteus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamine + H2O | - |
Micrococcus luteus | L-glutamate + NH3 | - |
? | |
L-glutamine + H2O | - |
Micrococcus luteus K-3 | L-glutamate + NH3 | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 48000, full-length enzyme, SDS-PAGE, 2 * 42000, C-terminally truncated enzyme, SDS-PAGE | Micrococcus luteus |
More | The glutaminase fragment is composed of N-terminal and C-terminal domains, and a putative catalytic dyad of S64 and K67 is located in a cleft of the N-terminal domain | Micrococcus luteus |
Synonyms | Comment | Organism |
---|---|---|
salt-tolerant glutaminase | - |
Micrococcus luteus |