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3.5.1.2: glutaminase

This is an abbreviated version!
For detailed information about glutaminase, go to the full flat file.

Word Map on EC 3.5.1.2

Reaction

L-glutamine
+
H2O
=
L-glutamate
 +
NH3

Synonyms

AnsB, AoGls, GA, GAB, GAC, GahB, GLA, GLNase, GLS, GLS1, GLS2, GlsA, glutaminase, glutaminase 1, glutaminase 2, glutaminase A, glutaminase B, glutaminase C, glutaminase I, glutaminase K, glutaminase L, glutaminase-1, glutaminase-2, glutaminase-B, glutamine amidohydrolase, glutamine aminohydrolase, glutamine deamidating enzyme, K-glutaminase, KAG, KGA, kidney-type glutaminase, kidney-type-glutaminase, L-glutaminase, L-glutamine amidohydrolase, LAG, LGA, liver-type glitaminase, liver-type glutaminase, Mglu, Micrococcus glutaminase Mglu, Micrococcus luteus K-3-type glutaminase, mitochondrial glutaminase, N-PAG, neuroblastoma glutaminase, neuroblastoma PAG, Nit 2, nitrilase 2, omega-amidase, PAG, PDX2, phosphate activated glutaminase, phosphate-activated glutaminase, phosphate-activated L-glutamine amidohydrolase, salt-tolerant glutaminase, YaaE

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.2 glutaminase

Specific Activity

Specific Activity on EC 3.5.1.2 - glutaminase

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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.094
-
crude enzyme, at pH 8.6 and 37°C
0.502
-
crude extract, at pH 7.5 and 35°C
0.516
-
pH 7.5, 40°C, Lactobacillus reuteri shows the highest activity compared to wild-type Lactobacillus plantarum and wild-type Lactobacillus paracasei which are transformed with the glutaminase gene Lactobacillus reuteri in this study. The wild-type Lactobacillus paracasei shows no glutaminase activity
0.68
-
PAG, healthy liver tissue
0.912
-
after 9.7fold purification, at pH 8.6 and 37°C
1.23
-
recombinant enzyme
1.92
-
supernatant, at pH 6.5 and 60°C
102.3
Vmax apparent, no Michaelis-Menten kinetics
11.1
recombinant enzyme in Escherichia coli strain JM109
1230
-
purified native enzyme
1246
-
purified recombinant enzyme
16.3
-
with L-Leu-Gln-Gly as substrate, at pH 9.0 and 50°C
16.4
-
pH 7.5, 37°C
196.2
-
after 102.4fold purification, at pH 6.5 and 60°C
2.4
-
PAG, cirrhotic disease patient liver tissue
22.1
purified enzyme
236.2
-
with L-Ala-Gln as substrate, at pH 9.0 and 50°C
25.71
Vmax apparent, no Michaelis-Menten kinetics
27.1
purified enzyme
29.7
1 mol/l NaCl present
29.9
-
with Cbz-Gln-Gly as substrate, at pH 9.0 and 50°C
308.3
-
with Gly-Gln as substrate, at pH 9.0 and 50°C
32.4
-
with Cbz-L-Gln as substrate, at pH 9.0 and 50°C
36.45
-
polyacrylic acid-Cu2+-immobilized enzyme, at pH 8.0 and 50°C
40.32
-
free enzyme, at pH 8.0 and 50°C
403
-
recombinant enzyme with N-terminal deletion
405
-
recombinant enzyme with N-terminal and C-terminal deletions
50.6
-
with D-asparagine as substrate, at pH 9.0 and 50°C
51
-
pH 7.0, 37°C
58.6
-
pH 7.0, 37°C
584.2
-
purified enzyme, pH 11.0, 70°C
613.3
-
pH 7.0, 30°C
7.44
-
after 14.8fold purification, at pH 7.5 and 35°C
720.5
-
with L-glutamine as substrate, at pH 9.0 and 50°C
73.2
-
with L-Pro-Leu-Gly-Gln as substrate, at pH 9.0 and 50°C
730
purified recombinant enzyme
additional information