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Literature summary for 2.3.2.2 extracted from

  • Kimura, K.; Tran, L.S.; Uchida, I.; Itoh, Y.
    Characterization of Bacillus subtilis gamma-glutamyltransferase and its involvement in the degradation of capsule poly-gamma-glutamate (2004), Microbiology, 150, 4115-4123.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
poly(gamma-glutamic acid) + H2O Bacillus subtilis the enzyme is involved in the degradation of capsule poly-gamma-glutamate to supply stationary-phase cells with constituent glutamates. Successive hydrolysis from the amino-terminal end D-Glu + L-Glu
-
?
poly(gamma-glutamic acid) + H2O Bacillus subtilis NAFM5 the enzyme is involved in the degradation of capsule poly-gamma-glutamate to supply stationary-phase cells with constituent glutamates. Successive hydrolysis from the amino-terminal end D-Glu + L-Glu
-
?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis Q83XQ6 NAFM5
-
Bacillus subtilis NAFM5 Q83XQ6 NAFM5
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
poly(gamma-glutamic acid) + H2O the enzyme is involved in the degradation of capsule poly-gamma-glutamate to supply stationary-phase cells with constituent glutamates. Successive hydrolysis from the amino-terminal end Bacillus subtilis D-Glu + L-Glu
-
?
poly(gamma-glutamic acid) + H2O successive hydrolysis from the amino-terminal end Bacillus subtilis D-Glu + L-Glu
-
?
poly(gamma-glutamic acid) + H2O the enzyme is involved in the degradation of capsule poly-gamma-glutamate to supply stationary-phase cells with constituent glutamates. Successive hydrolysis from the amino-terminal end Bacillus subtilis NAFM5 D-Glu + L-Glu
-
?
poly(gamma-glutamic acid) + H2O successive hydrolysis from the amino-terminal end Bacillus subtilis NAFM5 D-Glu + L-Glu
-
?