Literature summary for 3.4.19.13 extracted from

Boanca, G.; Sand, A.; Okada, T.; Suzuki, H.; Kumagai, H.; Fukuyama, K.; Barycki, J.J.
Autoprocessing of Helicobacter pylori gamma-glutamyltranspeptidase leads to the formation of a threonine-threonine catalytic dyad (2007), J. Biol. Chem., 282, 534-541.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
to 1.9 A resolution. The refined model contains two 40-kDa/20-kDa heterodimers in the asymmetric unit and has structural features comparable with other N-terminal nucleophile hydrolases. Autoprocessing of the enzyme leads to a large conformational change, with the loop preceding the catalytic residue Thr380 moving more than 35 A, thus relieving steric constraints that likely limit substrate binding. Cleavage of the proenzyme results in the formation of a threonine-threonine dyad comprised of Thr380 and Thr398. The hydroxyl group of Thr398 is located equidistant from the alpha-amino group and hydroxyl side chain of Thr380	Helicobacter pylori

Crystallization (Comment)

Organism

to 1.9 A resolution. The refined model contains two 40-kDa/20-kDa heterodimers in the asymmetric unit and has structural features comparable with other N-terminal nucleophile hydrolases. Autoprocessing of the enzyme leads to a large conformational change, with the loop preceding the catalytic residue Thr380 moving more than 35 A, thus relieving steric constraints that likely limit substrate binding. Cleavage of the proenzyme results in the formation of a threonine-threonine dyad comprised of Thr380 and Thr398. The hydroxyl group of Thr398 is located equidistant from the alpha-amino group and hydroxyl side chain of Thr380

Helicobacter pylori

Protein Variants

Protein Variants	Comment	Organism
T398A	mutation results in an enzyme that is fully capable of autoprocessing but is devoid of enzymatic activity	Helicobacter pylori
T398S	retains considerable enzymatic activity, but hydrolysis rates are reduced about 5fold relative to wild-type enzyme and overall catalyticefficiency is diminished by nearly an order of magnitude	Helicobacter pylori

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0125	-	L-glutamic acid-(4-nitroanilide)	wild-type, pH 8.0, 25°C	Helicobacter pylori
0.0203	-	L-glutamic acid-(4-nitroanilide)	mutant T398S, pH 8.0, 25°C	Helicobacter pylori

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
20000	-	1 * 40000, plus 1 * 20000, SDS-PAGE	Helicobacter pylori
40000	-	1 * 40000, plus 1 * 20000, SDS-PAGE	Helicobacter pylori

Organism

Organism	UniProt	Comment	Textmining
Helicobacter pylori	O25743	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	enzyme is expressed as a 60-kDa inactive precursor that must undergo autocatalytic processing to generate a 40-kDa/20-kDa heterodimer with full gamma-glutamyl amide bond hydrolase activity. The new N-terminus of the processed enzyme, Thr380, is the catalytic nucleophile in both the autoprocessing and enzymatic reactions	Helicobacter pylori

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-glutamic acid-(4-nitroanilide) + H2O	-	Helicobacter pylori	4-nitroaniline + L-glutamate	-	?

Subunits

Subunits	Comment	Organism
dimer	1 * 40000, plus 1 * 20000, SDS-PAGE	Helicobacter pylori