Characterization and sequence of a cDNA clone of gamma-glutamyltranspeptidase

Coloma, Julio; Pitot, Henry C.

doi:10.1093/nar/14.3.1393

Cited by 69 publications

(42 citation statements)

References 30 publications

(20 reference statements)

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“…The N-terminal sequence of GGT-A subunit I had a 88,81, 50, 50, and 31 % sequence identity to that of the light subunit from B. subtilis SJl38,9) B. subtilis (natto) NR-l,8) E. coli K_12,25) Pseudomonas sp. A14,7) and rat kidney, 26) respectiverly. Thesequence ofGGT-A and GGT-B subunit II had a 63, 50, 38, 31, and 19% sequence identity to the corresponding sequences of heavy subunit from SJl38, NR-L K-12, A14, and rat kindey, respectively.…”

Section: Discussionmentioning

confidence: 99%

Purification and Properties of Two Isozymes of γ-Glutamyltranspeptidase fromBacillus subtilisTAM-4

Abe

Ito

Ohmachi

et al. 1997

Bioscience, Biotechnology, and Biochemistry

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Section: Discussionmentioning

confidence: 99%

Purification and Properties of Two Isozymes of γ-Glutamyltranspeptidase fromBacillus subtilisTAM-4

Abe

Ito

Ohmachi

et al. 1997

Bioscience, Biotechnology, and Biochemistry

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“…Rat kidney and liver cDNAs appear to be almost identical in the nucleotide sequence of their coding regions but differ in their 5' untranslated region. Therefore, they probably originated through alternative splicing from a single locus (7)(8)(9).…”

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confidence: 99%

Identification of a human gamma-glutamyl cleaving enzyme related to, but distinct from, gamma-glutamyl transpeptidase.

Heisterkamp

Meyts

Uribe

et al. 1991

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

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We have cloned a 2.4-kilobase cDNA from a human placental cDNA library by using a y-glutamyl transpeptidase [GGT; y-glutamyltransferase, (5-glutamyl)-peptide:amino acid 5-glutamyltransferase, EC 2.3.2.2] probe. The deduced amino acid sequence of this cDNA, GGT-rel, exhibited an overall similarity of 39.5% with human GGT. Sequences that could represent a heavy and a light chain, analogous to GGT, as well as a putative transmembrane region were identified in GGT-rel. Transfectants overexpressing GGT-rel were tested for their ability to catalyze cleavage of the y-glutamyl moiety from natural and synthetic substrates for GGT. Experiments with glutathione added to the medium suggested that GGT-rel could hydrolyze the r-glutamyl moiety.More definitive evidence was obtained in experiments in which this protein converted leukotriene C4 to leukotriene D4. However, GGT-rel did not convert synthetic substrates that are commonly used to assay GGT. Our results indicate that GGT can no longer be considered the only enzyme capable of cleaving the y-glutamyl linkage of leukotriene C4 and, most likely, of other natural compounds.y-Glutamyl transpeptidase [GGT; y-glutamyltransferase, (5-glutamyl)-peptide:amino acid 5-glutamyltransferase, EC 2.3.2.2] is one of the major enzymes involved in the metabolism of glutathione (L-y-glutamyl-

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“…This kind of processing is very rare in procaryotes, but some examples have been reported (21,24,31). In the case of penicillin acylase, a spacer sequence between two subunits is known (21, 24), but that kind of sequence was not reported in E. coli S-adenosylmethionine decarboxylase (31) and mammalian GGTs (5,10,15,17,22). Since the molecular weight of the large subunit of E. coli GGT was 39,200 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis (28), which coincides with the molecular weight calculated from the sequence data (39197.68), the proteolytic cleavage is thought to occur only between Gln-390 and Thr-391 and between Ala-25 and Ala-26.…”

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confidence: 99%

“…The cDNA of rat renal GGT was cloned, and its nucleotide sequence was determined by Laperche et al (15) and Coloma and Pitot (5), respectively. More recently, Sakamuro et al (22) cloned the cDNA of human hepatic GGT, Meyts et al (17) cloned that of human placental GGT, Goodspeed et al (10) cloned that of human hepatoma GGT, and the nucleotide sequences were determined.…”

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confidence: 99%

“…This kind of processing is very rare in procaryotes, but some examples have been reported (21,24,31). In the case of penicillin acylase, a spacer sequence between two subunits is known (21,24), but that kind of sequence was not reported in E. coli S-adenosylmethionine decarboxylase (31) and mammalian GGTs (5,10,15,17,22 No DNA sequence showing high similarity with the consensus sequence for the u70 promoter was found at the N terminus. Since E. coli GGT is best expressed at 20°C and is expressed only very weakly at 37°C (29), it might be one of the cold shock proteins (13).…”

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DNA sequence of the Escherichia coli K-12 gamma-glutamyltranspeptidase gene, ggt

et al. 1989

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The DNA sequence of ggt, the gene that codes for -y-glutamyltranspeptidase (EC 2.3.2.2) of Escherichia coli K-12, has been determined. The sequence contains a single open reading frame encoding the signal peptide and large and small subunits, in that order. This result suggests that E. coli y-glutamyltranspeptidase is processed posttranslationally.-y-Glutamyltranspeptidase (GGT) ( (29), but the mechanism of its regulation remains to be elucidated.GGT consists of one large and one small subunit (18,28,34). Mammalian GGTs are synthesized as single propolypeptides and then processed into large and small subunits (9,16,19,20). It was of interest to us to determine whether E. coli GGT is also synthesized as a single polypeptide and processed later.To obtain information on these points, we performed DNA sequencing of E. coli K-12 ggt in this study.The nucleotide sequence of E. coli DNA inserted in pSH101 (27) was determined in both directions by the M13 dideoxy-sequencing method (23,26,35) Fig. 1. The large subunit is located proximal to the N terminus and the small subunit is distal to it. We looked upstream for the possible initiation codon, Shine-Dalgarno sequence (25), and promoter; the likeliest ones are shown in Fig. 1 (2,3,9,16,19,20,32). This kind of processing is very rare in procaryotes, but some examples have been reported (21,24,31). In the case of penicillin acylase, a spacer sequence between two subunits is known (21, 24), but that kind of sequence was not reported in E. coli S-adenosylmethionine decarboxylase (31) and mammalian GGTs (5,10,15,17,22). Since the molecular weight of the large subunit of E. coli GGT was 39,200 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis (28), which coincides with the molecular weight calculated from the sequence data (39197.68), the proteolytic cleavage is thought to occur only between Gln-390 and Thr-391 and between Ala-25 and Ala-26.The secondary structure at this site (Gln-390 and Thr-391) was calculated by the method of Chou and Fasman (4) to be a turn, which is preferentially recognized by signal peptidases (8). However, since signal peptidase II shows preferential cleavage between glycine and cysteine and since signal peptidase I prefers the C terminus of a signal peptide to be an amino acid with a small side chain, such as alanine, serine, or glycine (8), neither of these signal peptidases is likely to be the protease responsible for the cleavage between Gln-390 and Thr-391. More studies are needed to determine when, where, and how the processing into large and small subunits takes place and what kind of protease is responsible for this processing.A likely signal peptide consisting of 25 amino acids was found at the N terminus, with the cleavage occurring between No DNA sequence showing high similarity with the consensus sequence for the u70 promoter was found at the N terminus. Since E. coli GGT is best expressed at 20°C and is expressed only very weakly at 37°C (29), it might be one of the cold shock proteins (13). In E. coli, the heat sh...

show abstract

Characterization and sequence of a cDNA clone of gamma-glutamyltranspeptidase

Cited by 69 publications

References 30 publications

Purification and Properties of Two Isozymes of γ-Glutamyltranspeptidase fromBacillus subtilisTAM-4

Purification and Properties of Two Isozymes of γ-Glutamyltranspeptidase fromBacillus subtilisTAM-4

Identification of a human gamma-glutamyl cleaving enzyme related to, but distinct from, gamma-glutamyl transpeptidase.

DNA sequence of the Escherichia coli K-12 gamma-glutamyltranspeptidase gene, ggt

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