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Literature summary for 3.5.1.2 extracted from

  • Yoshimune, K.; Yamashita, R.; Masuo, N.; Wakayama, M.; Moriguchi, M.
    Digestion by serine proteases enhances salt tolerance of glutaminase in the marine bacterium Micrococcus luteus K-3 (2004), Extremophiles, 8, 441-446.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli strain JM109 Micrococcus luteus

Inhibitors

Inhibitors Comment Organism Structure
NaCl inhibits the enzyme slightly at 2.6 M, the enzyme is salt-tolerant, the C-terminally serine protease-cleaved enzyme fragment 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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3
-
L-glutamine pH 7.5, 30°C, full-length enzyme, in presence of 2.6 M NaCl Micrococcus luteus
3.7
-
L-glutamine pH 7.5, 30°C, protease-cleaved large enzyme fragment, in presence of 2.6 M NaCl Micrococcus luteus
3.8
-
L-glutamine pH 7.5, 30°C, protease-cleaved large enzyme fragment, in absence of NaCl Micrococcus luteus
6.1
-
L-glutamine pH 7.5, 30°C, full-length enzyme, in absence of NaCl Micrococcus luteus

Metals/Ions

Metals/Ions Comment Organism Structure
additional information the enzyme is salt-tolerant, the C-terminally serine protease-cleaved enzyme fragment 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 [Da] Molecular Weight Maximum [Da] Comment Organism
38500
-
1 * 48300, full-length enzyme, SDS-PAGE, 1 * 38500, N-terminal large enzyme fragment, after C-terminal cleavage by serine protease, SDS-PAGE Micrococcus luteus
38970
-
N-terminal large enzyme fragment comprising residues 1-368, MALDI-TOF mass spectrometry Micrococcus luteus
48300
-
1 * 48300, full-length enzyme, SDS-PAGE, 1 * 38500, N-terminal large enzyme fragment, after C-terminal cleavage by serine protease, SDS-PAGE Micrococcus luteus

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Micrococcus luteus
-
-
-
Micrococcus luteus K-3
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme from strain K-3 to homogeneity, recombinant enzyme from Escherichia coli strain JM109 by anion exchange chromatography to homogeneity Micrococcus luteus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1230
-
purified native enzyme Micrococcus luteus
1246
-
purified recombinant enzyme Micrococcus luteus

Substrates and Products (Substrate)

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

Subunits Comment Organism
monomer 1 * 48300, full-length enzyme, SDS-PAGE, 1 * 38500, N-terminal large enzyme fragment, after C-terminal cleavage by serine protease, SDS-PAGE Micrococcus luteus

Synonyms

Synonyms Comment Organism
salt-tolerant glutaminase
-
Micrococcus luteus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Micrococcus luteus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
128
-
L-glutamine pH 7.5, 30°C, full-length enzyme, in presence of 2.6 M NaCl Micrococcus luteus
403.3
-
L-glutamine pH 7.5, 30°C, full-length enzyme, in presence of 2.6 M NaCl Micrococcus luteus
821.7
-
L-glutamine pH 7.5, 30°C, protease-cleaved large enzyme fragment, in presence of 2.6 M NaCl Micrococcus luteus
873.3
-
L-glutamine pH 7.5, 30°C, protease-cleaved large enzyme fragment, in absence of NaCl Micrococcus luteus
1373
-
L-glutamine pH 7.5, 30°C, full-length enzyme, in absence of NaCl Micrococcus luteus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Micrococcus luteus