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Literature summary for 3.4.19.13 extracted from

  • Okada, T.; Suzuki, H.; Wada, K.; Kumagai, H.; Fukuyama, K.
    Crystal structure of the gamma-glutamyltranspeptidase precursor protein from Escherichia coli. Structural changes upon autocatalytic processing and implications for the maturation mechanism (2007), J. Biol. Chem., 282, 2433-2439.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
to 1.95 A resolution. The enzyme has a stacked alphabetabetaalpha fold comprising the large and small subunits, similar to the folds seen in members of the N-terminal nucleophile hydrolase superfamily. The active site residue Thr391, the N-terminal residue of the small subunit, is located in the groove, from which the pocket for gamma-glutamyl moiety binding follows. The gamma-glutamyl-enzyme intermediate and the structure of the complex with L-glutamate reveal how the gamma-glutamyl moiety and L-glutamate are recognized by the enzyme. A water molecule is seen on the carbonyl carbon of the gamma-glutamyl-Thr391 O bond in the intermediate that is to be hydrolyzed. The residues essential for enzymic activity, i.e. Arg114, Asp433, Ser462, and Ser463, are all involved in the binding of the gamma-glutamyl moiety Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P18956
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glutathione + H2O
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Escherichia coli L-cysteinylglycine + L-glutamate the reaction consists of two steps. First the active O atom of Thr391 attacks the carbonyl carbon atom of the gamma-glutamyl compound to form the gamma-glutamyl-enzyme intermediate, and then the gamma-glutamyl moiety is transferred to another substrate, i.e. reaction of EC 2.3.2.2, or the gamma-glutamyl-enzyme bond is hydrolyzed to reform the resting enzyme. The second step of the reaction, the hydrolysis of the intermediate, is much slower than the first reaction step ?