γ-Glutamyl transpeptidase: catalytic, structural and functional aspects

Tate, Suresh S.; Meister, Alton

doi:10.1007/bf00232585

Cited by 422 publications

(172 citation statements)

References 96 publications

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“…These molecules were shown by tandem ESI-MS to be the dipeptide cysteinylglycine (Fig. 6 C and D), a compound normally produced in mammals by intracellular metabolism of glutathione (29). Thus, we conclude that the intermediates 1 and 2 are monocysteinylglycine-heme and dicysteinylglycine-heme, respectively.…”

Section: Resultsmentioning

confidence: 63%

A heme-degradation pathway in a blood-sucking insect

Paiva-Silva

Cruz-Oliveira

Nakayasu

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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Hematophagous insects are vectors of diseases that affect hundreds of millions of people worldwide. A common physiological event in the life of these insects is the hydrolysis of host hemoglobin in the digestive tract, leading to a massive release of heme, a known prooxidant molecule. Diverse organisms, from bacteria to plants, express the enzyme heme oxygenase, which catalyzes the oxidative degradation of heme to biliverdin (BV) IX, CO, and iron. Here, we show that the kissing bug Rhodnius prolixus, a vector of Chagas' disease, has a unique heme-degradation pathway wherein heme is first modified by addition of two cysteinylglycine residues before cleavage of the porphyrin ring, followed by trimming of the dipeptides. Furthermore, in contrast to most known heme oxygenases, which generate BV IX␣, in this insect, the end product of heme detoxification is a dicysteinyl-BV IX␥. Based on these results, we propose a heme metabolizing pathway that includes the identified intermediates produced during modification and cleavage of the heme porphyrin ring.biliverdin ͉ heme oxygenase ͉ oxidative stress ͉ Rhodnius

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Section: Resultsmentioning

confidence: 63%

A heme-degradation pathway in a blood-sucking insect

Paiva-Silva

Cruz-Oliveira

Nakayasu

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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“…GGT catalyzes the transfer of γ-glutamyl moiety from γ-glutamyl compounds to amino acids and peptides, and the hydrolysis of γ-glutamyl compounds (Tate & Meister, 1981). The enzymatic reaction catalyzed by GGT proceeds via a γ-glutamyl enzyme intermediate.…”

Section: Introductionmentioning

confidence: 99%

Increase of “Umami” and “Kokumi” Compounds in Miso, Fermented Soybeans, by the Addition of Bacterial γ-Glutamyltranspeptidase

Suzuki

2013

Int. J. Food Stud.

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γ-Glutamyltranspeptidase (GGT) hydrolyzes γ-glutamyl compounds and transfers their γ-glutamyl moieties to amino acids and peptides. We previously showed that the "umami" taste of soy sauce could be improved by the addition of salt-tolerant Bacillus subtilis GGT to the fermentation mixture, "moromi". Although miso fermentation is a semi-solid fermentation, unlike soy sauce fermentation, this was also the case. When 15 units of purified B. subtilis GGT were added to 418 g miso "moromi" (fermentation mixture), the glutamate concentration in "moromi" became 20 mM higher and the "umami" taste became stronger than without the addition of GGT after 2 to 6 months of fermentation. In addition, γ-Glu-Val and γ-Glu-Val-Gly, which are known as "kokumi" peptides, were identified in "tamari", and the concentrations of these γ-glutamyl peptides in "tamari" fermented by the addition of GGT were significantly higher than those of "moromi" without the addition of GGT. These results indicate that B. subtilis GGT is able to improve the taste of miso.

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“…T he enzyme ␥-glutamyltranspeptidase (GGT; EC 2.3.2.2) catalyzes the cleavage of the ␥-glutamyl linkage of ␥-glutamyl compounds, e.g., glutathione (GSH), and the transfer of their ␥-glutamyl group to other amino acids and peptides (1). The reaction catalyzed by GGT has been thought to proceed via a ␥-glutamyl-enzyme intermediate followed by nucleophilic substitution by water, amino acids, or peptides (Scheme 1).…”

mentioning

confidence: 99%

Crystal structures of γ-glutamyltranspeptidase from Escherichia coli , a key enzyme in glutathione metabolism, and its reaction intermediate

Okada

Suzuki

Wada

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

158

211

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␥-Glutamyltranspeptidase (GGT) is a heterodimic enzyme that is generated from the precursor protein through posttranslational processing and catalyzes the hydrolysis of ␥-glutamyl bonds in ␥-glutamyl compounds such as glutathione and͞or the transfer of the ␥-glutamyl group to other amino acids and peptides. We have determined the crystal structure of GGT from Escherichia coli K-12 at 1.95 Å resolution. GGT has a stacked ␣␤␤␣ fold comprising the large and small subunits, similar to the folds seen in members of the N-terminal nucleophile hydrolase superfamily. The active site Thr-391, the N-terminal residue of the small subunit, is located in the groove, from which the pocket for ␥-glutamyl moiety binding follows. We have further determined the structure of the ␥-glutamyl

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γ-Glutamyl transpeptidase: catalytic, structural and functional aspects

Cited by 422 publications

References 96 publications

A heme-degradation pathway in a blood-sucking insect

A heme-degradation pathway in a blood-sucking insect

Increase of “Umami” and “Kokumi” Compounds in Miso, Fermented Soybeans, by the Addition of Bacterial γ-Glutamyltranspeptidase

Crystal structures of γ-glutamyltranspeptidase from Escherichia coli , a key enzyme in glutathione metabolism, and its reaction intermediate

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