Amphibian embryo glutathione transferase: amino acid sequence and structural properties

Sacchetta, Paolo; Petruzzelli, Raffaele; Melino, Sonia; Bucciarelli, Tonino; Pennelli, A; Amicarelli, Fernanda; Miranda, Marta; Ilio, Carmine Di

doi:10.1042/bj3220679

Cited by 10 publications

(3 citation statements)

References 19 publications

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“…In comparison with mammalian GSTs, relatively little information is available on amphibian GSTs. Two distinct Pi-class GSTs, named BbGSTP1-1 [8,9] and BbGSTP2-2 [10,11] respectively, have been purified and characterized from the common toad (Bufo bufo) in our laboratory. BbGSTP1-1 is expressed at high level in embryo tissues during its early developmental stages [12,13].…”

Section: Introductionmentioning

confidence: 99%

A novel amphibian Pi-class glutathione transferase isoenzyme from Xenopus laevis: importance of phenylalanine 111 in the H-site

Luca

Favaloro

Carletti

et al. 2003

Biochemical Journal

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Screening of a liver tumour cDNA library from Xenopus laevis resulted in the isolation of a full-length cDNA clone encoding a novel Pi-class amphibian glutathione transferase (GST) isoenzyme (designated as XlGSTP1-1). The gene encodes a protein of 212 amino acids with a calculated molecular mass of 24428 Da. The product of the gene has been overexpressed in Escherichia coli and characterized. XlGSTP1-1 has one of the highest specific activities towards 1-chloro-2,4-dinitrobenzene (1310 micromol/min per mg of protein) obtained with any GST. A notable feature of XlGSTP1-1 is the presence in the H-site of Phe(111) and Pro(208) in place of tyrosine and glycine residues respectively, present in other mammalian Pi-class GSTs. Site-directed mutagenesis indicate that Phe(111) is involved in substrate specificity of XlGSTP1-1. We provide evidence showing that XlGSTP1-1 is present only in the embryo and its expression might be associated with cellular proliferation.

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Section: Introductionmentioning

confidence: 99%

A novel amphibian Pi-class glutathione transferase isoenzyme from Xenopus laevis: importance of phenylalanine 111 in the H-site

Luca

Favaloro

Carletti

et al. 2003

Biochemical Journal

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“…Compared with mammalian GSTs, relatively little information is available on the structural and functional properties of GSTs occurring in amphibia. We have previously purified and characterized a Pi-class isoenzyme, named bbGSTP1-1, from the common toad Bufo bufo in an early developmental stage [12,13]. Further studies from our laboratory revealed that bbGSTP1-1 declines to a very low level in adult liver [14].…”

Section: Introductionmentioning

confidence: 99%

Mu-class glutathione transferase from Xenopus laevis: molecular cloning, expression and site-directed mutagenesis

Luca

Favaloro

Angelucci

et al. 2002

Biochemical Journal

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A cDNA encoding a Mu-class glutathione transferase (XlGSTM1-1) has been isolated from a Xenopus laevis liver library, and its nucleotide sequence has been determined. XlGSTM1-1 is composed of 219 amino acid residues with a calculated molecular mass of 25359 Da. Unlike many mammalian Mu-class GSTs, XlGSTM1-1 has a narrow spectrum of substrate specificity and it is also less effective in conjugating 1-chloro-2,4-dinitrobenzene. A notable structural feature of XlGSTM1-1 is the presence of the Cys-139 residue in place of the Glu-139, as well as the absence of the Cys-114 residue, present in other Mu-class GSTs, which is replaced by Ala. Site-directed mutagenesis experiments indicate that Cys-139 is not involved in the catalytic mechanism of XlGSTM1-1 but may be in part responsible for its structural instability, and experiments in vivo confirmed the role of this residue in stability. Evidence indicating that Arg-107 is essential for the 1-chloro-2,4-dinitrobenzene conjugation capacity of XlGSTM1-1 is also presented.

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“…Compared with mammalian GSTs, relatively little is known about amphibian GSTs. Two immunologically different pi class GSTs (bbGSTP1-1 and bbGSTP2-2) have been isolated and characterised from the embryo and the liver of the common toad (Bufo bufo) (16,17 ). Both enzymes show structural and kinetic properties that distinguish them from orthologous mammalian GSTs (16,17 ).…”

Section: Introductionmentioning

confidence: 99%

Glutathione S‐Transferase, Similar to Sigma Class, from Skin Secretions of Xenopus laevis

Pennelli

Ortolano

Miele³

et al. 2000

IUBMB Life

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SummaryUsing glutathione af nity chromatography followed by isoelectrofocusing, we puri ed from the skin secretion of Xenopus laevis an isoenzyme of glutathione S-transferase with an apparent subunit molecular mass of 22.5 kDa and an isoelectric point at pH 5.1. Its N-terminal amino acid sequence was highly similar to that of the sigma class glutathione S-transferase, which previously was demonstrated to have a glutathione-dependent prostaglandin D 2 synthase activity. Immunohistochemistry analysis revealed that the isoenzyme was located in the cytoplasm of granular gland cells.

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Amphibian embryo glutathione transferase: amino acid sequence and structural properties

Cited by 10 publications

References 19 publications

A novel amphibian Pi-class glutathione transferase isoenzyme from Xenopus laevis: importance of phenylalanine 111 in the H-site

A novel amphibian Pi-class glutathione transferase isoenzyme from Xenopus laevis: importance of phenylalanine 111 in the H-site

Mu-class glutathione transferase from Xenopus laevis: molecular cloning, expression and site-directed mutagenesis

Glutathione S‐Transferase, Similar to Sigma Class, from Skin Secretions of Xenopus laevis

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