Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.5.1.2 extracted from

  • Yoshimune, K.; Shirakihara, Y.; Shiratori, A.; Wakayama, M.; Chantawannakul, P.; Moriguchi, M.
    Crystal structure of a major fragment of the salt-tolerant glutaminase from Micrococcus luteus K-3 (2006), Biochem. Biophys. Res. Commun., 346, 1118-1124.
    View publication on PubMed
Search for more literature for 3.5.1.2

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli strain JM109 Micrococcus luteus

Crystallization (Commentary)

Crystallization (Comment) Organism
C-terminally truncated enzyme, hanging-drop, vapor-diffusion method at 25°C, X-ray diffraction structure determination and analysis at 2.4 resolution using multiple-wavelength anomalous dispersion, MAD Micrococcus luteus

Protein Variants

Protein Variants Comment Organism
K67E site-directed mutagenesis, catalytic residue mutant, inactiv Micrococcus luteus
S64A site-directed mutagenesis, catalytic residue mutant, inactiv Micrococcus luteus

Metals/Ions

Metals/Ions Comment Organism Structure
additional information 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 Micrococcus luteus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
42000
-
 2 * 48000, full-length enzyme, SDS-PAGE, 2 * 42000, C-terminally truncated enzyme, SDS-PAGE Micrococcus luteus
48000
-
 2 * 48000, full-length enzyme, SDS-PAGE, 2 * 42000, C-terminally truncated enzyme, SDS-PAGE Micrococcus luteus
86000
-
 C-terminally truncated enzyme, gel filtration Micrococcus luteus
96000
-
 full-length enzyme, gel filtration 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
recombinant wild-type and mutant enzymes from Escherichia coli strain JM109 Micrococcus luteus

Reaction

Reaction Comment Organism Reaction ID
L-glutamine + H2O = L-glutamate + NH3 active site structure, the enzyme contains a catalytic dyad formed by S64 and K67 Micrococcus luteus
a

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
dimer 2 * 48000, full-length enzyme, SDS-PAGE, 2 * 42000, C-terminally truncated enzyme, SDS-PAGE Micrococcus luteus
More The glutaminase fragment is composed of N-terminal and C-terminal domains, and a putative catalytic dyad of S64 and K67 is located in a cleft of the N-terminal domain Micrococcus luteus

Synonyms

Synonyms Comment Organism
salt-tolerant glutaminase
-
 Micrococcus luteus