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Literature summary for 3.5.1.2 extracted from
- Purification and characterization of a glutaminase enzyme accounting for the majority of glutaminase activity in Aspergillus sojae under solid-state culture (2013), Appl. Microbiol. Biotechnol., 97, 8581-8590.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Aspergillus oryzae strain RIB40 RP-1 | Aspergillus sojae |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| NaCl | the enzyme activity is inhibited by approximately 95% in the presence of 18% (w/v) NaCl | Aspergillus sojae |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 66400 | - |
2 * 66400, deglycosylated enzyme, SDS-PAGE | Aspergillus sojae |
| 110000 | - |
2 * 110000, native enzyme, SDS-PAGE | Aspergillus sojae |
| 259000 | - |
gel filtration | Aspergillus sojae |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-glutamine + H2O | Aspergillus sojae | - |
L-glutamate + NH3 | - |
? | |
| additional information | Aspergillus sojae | the enzyme prefers free L-glutamine to free L-asparagine, C-terminal glutaminyl, and asparaginyl residues in peptides | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus sojae | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | - |
Aspergillus sojae |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 16.3 | - |
with L-Leu-Gln-Gly as substrate, at pH 9.0 and 50°C | Aspergillus sojae |
| 29.9 | - |
with Cbz-Gln-Gly as substrate, at pH 9.0 and 50°C | Aspergillus sojae |
| 32.4 | - |
with Cbz-L-Gln as substrate, at pH 9.0 and 50°C | Aspergillus sojae |
| 50.6 | - |
with D-asparagine as substrate, at pH 9.0 and 50°C | Aspergillus sojae |
| 73.2 | - |
with L-Pro-Leu-Gly-Gln as substrate, at pH 9.0 and 50°C | Aspergillus sojae |
| 236.2 | - |
with L-Ala-Gln as substrate, at pH 9.0 and 50°C | Aspergillus sojae |
| 308.3 | - |
with Gly-Gln as substrate, at pH 9.0 and 50°C | Aspergillus sojae |
| 720.5 | - |
with L-glutamine as substrate, at pH 9.0 and 50°C | Aspergillus sojae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Cbz-Gln-Gly + H2O | - |
Aspergillus sojae | Cbz-Glu-Gly + NH3 | - |
? | |
| Cbz-L-Gln + H2O | - |
Aspergillus sojae | Cbz-L-Glu + NH3 | - |
? | |
| D-asparagine + H2O | - |
Aspergillus sojae | D-aspartate + NH3 | - |
? | |
| Gly-Asn + H2O | - |
Aspergillus sojae | Gly-Asp + NH3 | - |
? | |
| Gly-Gln + H2O | - |
Aspergillus sojae | Gly-Glu + NH3 | - |
? | |
| L-Ala-Gln + H2O | - |
Aspergillus sojae | L-Ala-L-Glu + NH3 | - |
? | |
| L-Asn + H2O | - |
Aspergillus sojae | L-Asp + NH3 | - |
? | |
| L-asparagine + H2O | - |
Aspergillus sojae | L-aspartate + NH3 | - |
? | |
| L-glutamine + H2O | - |
Aspergillus sojae | L-glutamate + NH3 | - |
? | |
| L-Leu-Ala-Asn + H2O | - |
Aspergillus sojae | L-Leu-Ala-Asp + NH3 | - |
? | |
| L-Leu-Gln-Gly + H2O | - |
Aspergillus sojae | L-Leu-Glu-Gly + NH3 | - |
? | |
| L-Leu-Gly-Asn + H2O | - |
Aspergillus sojae | L-Leu-Gly-Asp + NH3 | - |
? | |
| L-Pro-Leu-Gly-Asn + H2O | - |
Aspergillus sojae | L-Pro-Leu-Gly-Asp + NH3 | - |
? | |
| L-Pro-Leu-Gly-Gln + H2O | - |
Aspergillus sojae | L-Pro-Leu-Gly-Glu + NH3 | - |
? | |
| additional information | the enzyme prefers free L-glutamine to free L-asparagine, C-terminal glutaminyl, and asparaginyl residues in peptides | Aspergillus sojae | ? | - |
? | |
| additional information | the enzyme does not show any activity against L-Glu, D-Asn, L-Gln-Gly, gamma-glutamyl hydrazide, glutathione, and L-gamma-Glu-4-nitroanilide | Aspergillus sojae | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | 2 * 110000, native enzyme, SDS-PAGE | Aspergillus sojae |
| homodimer | 2 * 66400, deglycosylated enzyme, SDS-PAGE | Aspergillus sojae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GahB | - |
Aspergillus sojae |
| glutamine amidohydrolase | - |
Aspergillus sojae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
- |
Aspergillus sojae |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1606 | - |
L-asparagine | at pH 9.0 and 50°C | Aspergillus sojae | |
| 4790 | - |
Gly-Gln | at pH 9.0 and 50°C | Aspergillus sojae | |
| 6249 | - |
L-glutamine | at pH 9.0 and 50°C | Aspergillus sojae | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 9 | - |
- |
Aspergillus sojae |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 10 | the enzyme is stable in the range of pH4.0-10.0 at 30°C for 16 h | Aspergillus sojae |
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