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Literature summary for 2.3.2.2 extracted from

  • Ogawa, Y.; Hosoyama, H.; Hamano, M.; Motai, H.
    Purification and properties of gamma-glutamyltranspeptidase from Bacillus subtilis (natto) (1991), Agric. Biol. Chem., 55, 2971-2977.
    View publication on PubMed
Search for more literature for 2.3.2.2

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Bacillus subtilis
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 N-terminal sequence Bacillus subtilis
22000
-
 1 * 45000 + 1 * 22000, SDS-PAGE Bacillus subtilis
45000
-
 1 * 45000 + 1 * 22000, SDS-PAGE Bacillus subtilis
58000
-
 gel filtration Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
glutathione + an amino acid Bacillus subtilis involved in polyglutamic acid synthesis L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
 natto strain NR-1
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bacillus subtilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 activities with diverse substrates Bacillus subtilis
62.9
-
 purified enzyme Bacillus subtilis
81.5
-
 purified enzyme Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(5-L-glutamyl)-peptide + acceptor + H+ concurrent reaction: hydrolase reaction with H2O as acceptor Bacillus subtilis peptide + 5-L-glutamyl amino acid
-
 ?
(5-L-glutamyl)-peptide + acceptor + H+ donors are Glu, alpha-L-Glu-L-Ala Bacillus subtilis peptide + 5-L-glutamyl amino acid
-
 ?
(5-L-glutamyl)-peptide + acceptor + H+ dipeptides are better acceptors than free amino acids Bacillus subtilis peptide + 5-L-glutamyl amino acid
-
 ?
(5-L-glutamyl)-peptide + acceptor + H+ concurrent reaction: autotranspeptidation with another donor molecule as acceptor Bacillus subtilis peptide + 5-L-glutamyl amino acid
-
 ?
(5-L-glutamyl)-peptide + acceptor + H+ acceptor specificity, overview Bacillus subtilis peptide + 5-L-glutamyl amino acid
-
 ?
(5-L-glutamyl)-peptide + acceptor + H+ donor specificity, overview Bacillus subtilis peptide + 5-L-glutamyl amino acid
-
 ?
5-L-glutamine + 5-L-glutamine
-
 Bacillus subtilis 5-poly-glutamic acid + glutamate
-
 ?
5-L-glutamyglycylglycine + acceptor
-
 Bacillus subtilis glycylglycine + 5-L-glutamyl-acceptor
-
 ?
5-L-glutamyl-4-nitroanilide + glycylglycine
-
 Bacillus subtilis 4-nitroaniline + 5-L-glutamylglycylglycine
-
 ?
glutathione + an amino acid involved in polyglutamic acid synthesis Bacillus subtilis L-cysteinylglycine + a 5-L-glutamyl-amino acid
-
 ?

Subunits

Subunits Comment Organism
dimer 1 * 45000 + 1 * 22000, SDS-PAGE Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Bacillus subtilis
60
-
-
 Bacillus subtilis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
45 80 about half-maximal activity at 45°C and about 70% of maximal activity at 80°C Bacillus subtilis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
 at least 15 min stable Bacillus subtilis
55
-
 inactivation within 15 min at pH 8.0 Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
 Bacillus subtilis

pH Range

pH Minimum pH Maximum Comment Organism
7.5 9 about half-maximal activity at pH 7.5, about 90% of maximal activity at pH 9.0 Bacillus subtilis

pH Stability

pH Stability pH Stability Maximum Comment Organism
7 8 stable Bacillus subtilis