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Literature summary for 3.5.1.2 extracted from

  • Yoshimune, K.; Shirakihara, Y.; Wakayama, M.; Yumoto, I.
    Crystal structure of salt-tolerant glutaminase from Micrococcus luteus K-3 in the presence and absence of its product L-glutamate and its activator Tris (2010), FEBS J., 277, 738-748.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Tris activates Mglu by approximately 6fold at pH 7.5 Micrococcus luteus

Crystallization (Commentary)

Crystallization (Comment) Organism
determination of the structures of the intact enzyme in the presence and in the absence of its product L-glutamate and its activator Tris, which activates the enzyme by 6fold, and in the presence of both Micrococcus luteus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
48000
-
-
Micrococcus luteus

Organism

Organism UniProt Comment Textmining
Micrococcus luteus Q4U1A6 K-3
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamine + H2O strictly specific to L-glutamine Micrococcus luteus L-glutamate + NH3
-
?

Synonyms

Synonyms Comment Organism
Mglu
-
Micrococcus luteus
Micrococcus glutaminase Mglu
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Micrococcus luteus
salt-tolerant glutaminase
-
Micrococcus luteus

Temperature Optimum [°C]

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

pH Optimum

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