3.5.1.2: glutaminase

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

Reaction

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

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Results	in table
57	Activating Compound
97994	AA Sequence
21	Application
1	CAS Registry Number
37	Cloned(Commentary)
16	Crystallization (Commentary)
2155	Disease/ Diagnostics
8	Expression
13	General Information
7	General Stability
110	IC50 Value
272	Inhibitors
19	kcat/KM [mM/s]
14	Ki Value [mM]
103	KM Value [mM]
60	Localization
43	Metals/Ions
80	Molecular Weight [Da]
73	Natural Substrates/ Products (Substrates)
338	Organism
12	Pathway
188	PDB ID
55	pH Optimum
9	pH Range
9	pH Stability
2	pI Value
13	Posttranslational Modification
58	Protein Variants
51	Purification (Commentary)
5	Reaction
1	Reaction Type
150	Reference
154	Source Tissue
66	Specific Activity [micromol/min/mg]
13	Storage Stability
302	Substrates and Products (Substrate)
69	Subunits
172	Synonyms
1	Systematic Name
38	Temperature Optimum [°C]
6	Temperature Range [°C]
21	Temperature Stability [°C]
50	Turnover Number [1/s]

Metals Ions

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Metals Ions on EC 3.5.1.2 - glutaminase

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

arsenate

Sporosarcina pasteurii

-

50 mM, 800% of the relative activity without addition

655601

Ca2+

Rattus norvegicus

-

0.5-1.0 mM, 2fold activation of NEM-insensitive enzyme

209018

chloride

Homo sapiens

-

competes with phosphate for binding to the catalytic Ser291, at high concentration (500 mM NaCl) it can dislodge phosphate from its site and shift the protein equilibrium to lower-order oligomers

720930

Cl-

Triticale sp.

-

1 mM, markedly activates the enzyme

654234

K+

3 entries

KCl

2 entries

Na+

4 entries

NaBr

Micrococcus luteus

-

0.25 M, 1.2-1.3fold activation

209032

NaCl

9 entries

NaF

Micrococcus luteus

-

0.25 M, 1.2-1.3fold activation

209032

NaI

Micrococcus luteus

-

0.25 M, 1.2-1.3fold activation

209032

NH4+

Rhizobium etli

-

Ka 1 mM

654884

phosphate

5 entries

PO43-

2 entries

sulfate

Sporosarcina pasteurii

-

50 mM, 700% of the relative activity without addition

655601

additional information

7 entries

K+

Bacillus amyloliquefaciens

-

110% activity at 1 mM

733562

K+

Bacillus cereus

-

139.43% activity at 100 mM

733133

K+

Bacillus cereus

-

5 mM, 113% of initial activity

755231

KCl

Micrococcus luteus

-

2 M, 1.4fold activation

209032

KCl

Stenotrophomonas maltophilia

-

25% activation at 1 mM

669739

Na+

Aspergillus flavus

-

10 mM, 129% of initial activity

754315

Na+

Bacillus cereus

-

5 mM, 114% of initial activity

755231

Na+

Bacillus cereus

-

120.35% activity at 100 mM

733133

Na+

Synechocystis sp. PCC 6803

P73903

1 mol/l: 2fold activity

701208

NaCl

Bacillus sp. (in: Bacteria)

-

enhances activity at 1-20% w/v, but reduces activity by 30% at 25% w/v, optimal at 1%

718613

NaCl

Lacticaseibacillus rhamnosus

-

5%, increases activity almost 2fold

655373

NaCl

Limosilactobacillus reuteri

-

enzyme is salt-tolerant as the relative activity displays 110% in the condition of 5% NaCl and remains over 50% in the presence of 20% NaCl

710791

NaCl

Limosilactobacillus reuteri

-

salt-tolerant, 110% relative activity under 5% NaCl, 50% activity at 15% (w/v) concentration, over 50% activity with presence of 20% NaCl

710911

NaCl

Micrococcus luteus

-

8-16%, maximal activity of glutaminase I, no effect of glutaminase II

209026

NaCl

Penicillium palitans

-

75% of the original activity in the presence of 15-30% NaCl

713385

NaCl

Stenotrophomonas maltophilia

-

the enzyme is salt-tolerant, over 86% of maximal activity at 16% NaCl, no effect at 1 mM

669739

NaCl

Streptomyces sp.

-

optimum concentration 2%

753989

NaCl

Weissella cibaria

-

enzyme retains 40% of its activity in the presence of 15% NaCl, which is about 2fold higher than the activity of glutaminase from Aspergillus oryzae

710869

phosphate

Anabaena sp.

Q8YMZ9, Q8YSZ5

no activity without phosphate, max. activity at 60 mM K3PO4

697985

phosphate

Homo sapiens

-

activates the enzyme in vivo in tumor cells at 100 mM

667496

phosphate

Homo sapiens

-

phosphate-activated glutaminase isozyme

669694, 670129, 670391

phosphate

Rattus norvegicus

-

induces association to form active tetramers

657262

phosphate

Sporosarcina pasteurii

-

50 mM, 900% of the relative activity without addition

655601

PO43-

Bacillus cereus

-

143.13% activity at 100 mM

733133

PO43-

Triticale sp.

-

activity increases with the increase of the concentration of the ion

654234

additional information

Aspergillus oryzae

-

the enzyme from strain RIB40 is salt-tolerant, while the enzyme from strain MA-27-IM is salt-sensitive

669542

additional information

Bacillus amyloliquefaciens

-

not influenced by Mg2+, Zn2+, and Ni2+

733562

additional information

Micrococcus luteus

-

equivalent activities in absence and the presence of 3 M NaCl

654091

additional information

Micrococcus luteus

-

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

668534

additional information

Micrococcus luteus

-

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

667444

additional information

Sporosarcina pasteurii

-

no effect with NaCl, no significant alteration with KCl, MgCl2, MnCl2, CaCl2 and NH4Cl

655601

additional information

Stenotrophomonas maltophilia

-

the enzyme is not affected by NiCl2 at 1 mM

669739