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Literature summary extracted from

  • Ashiuchi, M.; Tani, K.; Soda, K.; Misono, H.
    Properties of glutamate racemase from Bacillus subtilis IFO 3336 producing poly-gamma-glutamate (1998), J. Biochem., 123, 1156-1163.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
5.1.1.3 additional information cofactor-independent enzyme Bacillus subtilis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.1.1.3 overexpression in Escherichia coli JM109 Bacillus subtilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.1.1.3 2-nitro-5-thiocyanatobenzoate 0.2 mM Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.1.1.3 2.5
-
D-glutamate pH 8.0, 37°C Bacillus subtilis
5.1.1.3 10
-
D-Homocysteinesulfinate pH 8.0, 37°C Bacillus subtilis
5.1.1.3 50
-
L-glutamate pH 8.0, 37°C Bacillus subtilis
5.1.1.3 200
-
L-Homocysteinesulfinate pH 8.0, 37°C Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.1.1.3 29866
-
1 * 29866, calculation from nucleotide sequence Bacillus subtilis
5.1.1.3 30000
-
-
Bacillus subtilis
5.1.1.3 30000
-
gel filtration Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.1.1.3 L-Glu Bacillus subtilis glutamate racemase is mainly concerned in D-Glu synthesis for poly-gamma-glutamate production ?
-
?
5.1.1.3 L-Glu Bacillus subtilis CU741 glutamate racemase is mainly concerned in D-Glu synthesis for poly-gamma-glutamate production ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
5.1.1.3 Bacillus subtilis
-
-
-
5.1.1.3 Bacillus subtilis
-
CU741
-
5.1.1.3 Bacillus subtilis
-
IFO 3336
-
5.1.1.3 Bacillus subtilis P94556 IFO 3336
-
5.1.1.3 Bacillus subtilis CU741
-
CU741
-
5.1.1.3 Pediococcus pentosaceus
-
IFO 3182
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.1.3
-
Bacillus subtilis

Source Tissue

EC Number Source Tissue Comment Organism Textmining
5.1.1.3 cell culture highest activity in the early stationary phase of growth Bacillus subtilis
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.1.1.3 42
-
-
Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.1.3 D-Glu
-
Bacillus subtilis L-Glu
-
?
5.1.1.3 D-Glu
-
Bacillus subtilis CU741 L-Glu
-
?
5.1.1.3 L-Glu glutamate racemase is mainly concerned in D-Glu synthesis for poly-gamma-glutamate production Bacillus subtilis ?
-
?
5.1.1.3 L-Glu glutamate racemase is mainly concerned in D-Glu synthesis for poly-gamma-glutamate production Bacillus subtilis CU741 ?
-
?
5.1.1.3 L-glutamate
-
Bacillus subtilis D-glutamate
-
?
5.1.1.3 L-Homocysteinesulfinate
-
Bacillus subtilis D-Homocysteinesulfinate
-
r

Subunits

EC Number Subunits Comment Organism
5.1.1.3 monomer 1 * 30000, SDS-PAGE Bacillus subtilis
5.1.1.3 monomer 1 * 30000 Bacillus subtilis
5.1.1.3 monomer 1 * 29866, calculation from nucleotide sequence Bacillus subtilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.1.1.3 37
-
-
Bacillus subtilis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
5.1.1.3 37
-
fully stable up to Bacillus subtilis
5.1.1.3 50
-
pH 8.0, 0.1 M Tris-HCl buffer containing 10% glycerol, retains 90% of its activity after 10 min Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.1.1.3 8
-
-
Bacillus subtilis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
5.1.1.3 7 10 enzyme shows significant activity in the range pH 7.0-10.0 Bacillus subtilis