Glutathionuria: γ‐Glutamyl transpeptidase deficiency

Wright, Elaine; Stern, Judith M.; Ersser, R. S.; Patrick, A. D.

doi:10.1007/bf01805554

Cited by 48 publications

(21 citation statements)

References 17 publications

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“…Inborn deficiency of GGT1 causes glutathionuria (Schulman et al 1975;Wright et al 1980). TGM1, also known as transglutaminase, is expressed during terminal differentiation of keratinocytes (Candi et al 1995); this enzyme synthesizes the cornified envelope by a cross-linking reaction (Melino et al 2000).…”

Section: Introductionmentioning

confidence: 99%

Catalog of 680 variations among eight cytochrome P450 (CYP) genes, nine esterase genes, and two other genes in the Japanese population

et al. 2003

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We screened DNAs from 48 Japanese individuals for single-nucleotide polymorphisms (SNPs) in eight cytochrome P450 (CYP) genes, nine esterase genes, and two other genes by directly sequencing the relevant genomic regions in their entirety except for repetitive elements. This approach identified 607 SNPs and 73 insertion/deletion polymorphisms among the 19 genes examined. Of the 607 SNPs, 284 were identified in CYP genes, 302 in esterase genes, and 21 in the other two genes (GGT1, and TGM1); overall, 37 SNPs were located in 5' flanking regions, 496 in introns, 55 in exons, and 19 in 3' flanking regions. These variants should contribute to studies designed to investigate possible correlations between genotypes and phenotypes of disease susceptibility or responsiveness to drug therapy.Keywords Single-nucleotide polymorphism (SNP) AE Cytochrome P450 (CYP) AE Esterase AE GGT1 AE TGM1

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Section: Introductionmentioning

confidence: 99%

Catalog of 680 variations among eight cytochrome P450 (CYP) genes, nine esterase genes, and two other genes in the Japanese population

et al. 2003

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“…In mammals, GGT is involved in the conversion of leukotriene C 4 to D 4 , although GGT is not the only enzyme that catalyzes this reaction (6,7). GGT is a key enzyme in glutathione metabolism, and genetic diseases of GGT deficiency, including glutathionemia and glutathionuria, are associated with mental retardation (8,9).…”

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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.

155

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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“…GGT knockout mice and the human subjects with GGT deficiency or single nucleotide polymorphism (SNP) would be good models for such studies. Fortunately, the human GGT deficiency, which is associated with mental retardation, is apparently very rare and only several cases have been reported (70)(71)(72)(73)(74), while there is no report of SNPs for human GGT so far. Another important aspect for future study is the regulation of GGT genes, especially in humans.…”

Section: Future Perspectivementioning

confidence: 99%

Redox Regulation of γ-Glutamyl Transpeptidase

Zhang

Forman

2009

Am J Respir Cell Mol Biol

135

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g-Glutamyl transpeptidase (GGT) catalyzes the transfer of the glutamyl moiety from glutathione, and glutathione S-conjugates to acceptors to form another amide or to water to produce free glutamate. Functionally, GGT plays important roles in glutathione homeostasis and mercapturic acid metabolism. The expression of GGT is increased as an adaptive response upon the exposure of oxidative stress. The underlying mechanism of this, however, is nebulous, as GGT gene structure is complex and its transcription is usually controlled by multiple promoters that generate several subtypes of GGT mRNAs. Studies reveal that signaling pathways such as Ras, ERK, p38MAPK, and PI3K are involved in the induction of GGT gene expression in response to oxidative stress. Thus, not surprisingly, induction of GGT mRNA subtypes and the involvement of multiple signaling pathways vary depending on cell type and stimuli.

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Glutathionuria: γ‐Glutamyl transpeptidase deficiency

Cited by 48 publications

References 17 publications

Catalog of 680 variations among eight cytochrome P450 (CYP) genes, nine esterase genes, and two other genes in the Japanese population

Catalog of 680 variations among eight cytochrome P450 (CYP) genes, nine esterase genes, and two other genes in the Japanese population

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

Redox Regulation of γ-Glutamyl Transpeptidase

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