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Literature summary for 3.5.1.2 extracted from

  • Weingand-Ziade, A.; Gerber-Decombaz, C.; Affolter, M.
    Functional characterization of a salt- and thermotolerant glutaminase from Lactobacillus rhamnosus (2003), Enzyme Microb. Technol., 32, 862-867.
No PubMed abstract available

Application

Application Comment Organism
additional information production of enzymically hydrolyzed plant proteins to reach high glutamic acid yields Lacticaseibacillus rhamnosus

Inhibitors

Inhibitors Comment Organism Structure
NaCl 15%, remains 90% of the initial activity Lacticaseibacillus rhamnosus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics Lacticaseibacillus rhamnosus
4.8
-
glutamine at 50ºC, pH 7.0 Lacticaseibacillus rhamnosus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Lacticaseibacillus rhamnosus 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
NaCl 5%, increases activity almost 2fold Lacticaseibacillus rhamnosus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-glutamine + H2O Lacticaseibacillus rhamnosus
-
L-glutamate + NH3
-
?

Organism

Organism UniProt Comment Textmining
Lacticaseibacillus rhamnosus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamine + H2O
-
Lacticaseibacillus rhamnosus L-glutamate + NH3
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
Lacticaseibacillus rhamnosus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
Lacticaseibacillus rhamnosus