Nucleotide sequence of a class μ glutathione S-transferase from chicken liver

Liu, Li‐Fan; Tam, Ming F.

doi:10.1016/0167-4781(91)90199-v

Cited by 28 publications

(20 citation statements)

References 13 publications

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“…The presence of multiple GST isozymes in chicken liver was first reported by Yeung and Gidari in 1980 (22). However, it was not until the 1990s that the structure of chicken GSTs at the protein and DNA sequence levels began to be elucidated (23)(24)(25)(26)(27), but little is known about these enzymes in avian species other than the domestic chicken.…”

Section: Tissue Collection and Sample Preparationmentioning

confidence: 98%

Glutathione S-transferases in the Japanese quail: Tissue distribution and purification of the liver isozymes

Dai

Edens

Roe

1996

J. Biochem. Toxicol.

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Section: Tissue Collection and Sample Preparationmentioning

confidence: 98%

Glutathione S-transferases in the Japanese quail: Tissue distribution and purification of the liver isozymes

Dai

Edens

Roe

1996

J. Biochem. Toxicol.

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“…A more flexible C-terminal tail near the active site is likely to a refers to an a-helix, and , 8 to a /3-strand. The references for the sequences are: hGSTAl [71], hGSTA2 [72], rGSTAla [73], rCSTA2 [74], rGSTA3 [75], mGSTAl [76], rbGSTAl [77], rGSTMl [78], rGSTM2 [79], rGSTM3 [80], h G S T M l b [81], mGSTMl [82], mCSTM2 [82], c G S T M 2 [83], g p C S T M [84], pGSTPl [31], hGSTPl [85], rGSTPl [86], bGSTPl [31], and mGSTPl [87]. The prefixes are defined as follows: h, human; r, rat; m, mouse; rb, rabbit; c, chicken; gp, guinea pig; p. pig; b, bovine.…”

Section: H-site and The Binding Of Electrophilesmentioning

confidence: 99%

X‐ray crystal structures of cytosolic glutathione S‐transferases

Dirr

Reinemer

Huber

1994

European Journal of Biochemistry

417

321

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Crystal structures of cytosolic glutathione S-transferases (EC 2.5.1.18), complexed with glutathione or its analogues, are reviewed. The atomic models define protein architectural relationships between the different gene classes in the superfamily, and reveal the molecular basis for substrate binding at the two adjacent subsites of the active site. Considerable progress has been made in understanding the mechanism whereby the thiol group of glutathione is destabilized (lowering its pK,) at the active site, a rate-enhancement strategy shared by the soluble glutathione S-transferases. Portrait of a superfamily of detoxification enzymesMany sophisticated defense strategies have evolved in organisms enabling them to deal with the constant threat by a broad spectrum of both foreign and endogenous cytotoxic and genotoxic compounds [1]. Enzyme systems that transact the chemical detoxification and elimination processes of these structurally diverse molecules, many of which are highly non-polar, can be divided into three major but interrelated groups; phase I enzymes, such as the cytochrome P450 superfamily, activate chemicals by forming reactive functional groups (e.g. epoxides) in them; phase I1 enzymes deactivate these reactive chemicals by appending a hydrophilic moiety (e.g. glutathionyl, glucuronyl, or sulphuryl) to the functional group ; phase Ill enzymes mediate the cellular elimination of the inactive and water-soluble products.The superfamily of glutathione S-transferases (EC 2.5.1.18) represents an integral part of the phase I1 detoxification mechanism. These intracellular proteins are found in most aerobic eukaryotes and prokaryotes, and protect cells against chemical-induced toxicity and stress by catalyzing the S-conjugation between the thiol group of glutathione and an electrophilic moiety in the hydrophobic and toxic sub- GST, glutathione S-transferase; pGSTP1-1, hGSTAl-1, rGSTM1-1 etc., acronyms for the glutathione S-transferases (GST), the prefix indicating the species (p, porcine; h, human ; r, rat; b, bovine; m, mouse; rb, rabbit; c, chicken; gp, guinea pig) while P, A, and M indicate gene class pi, alpha and mu, respectively ; 1-1 indicates a dimer of two type-1 subunits; GSH, reduced glutathione; P1, P2 etc. and G1, G2 etc., designate peptide functional groups in glutathione and the corresponding G-site ligands of the glutathione S-transferases, respectively; G-site, glutatbione-binding site; H-site, hydrophobic electrophile-binding site.Enzyme. Glutathione S-transferase (EC 2.5.1.1 8).strate. Glutathione S-transferases are perhaps the single most important family of enzymes involved in the metabolism of alkylating compounds [2]. The resultant glutathione S-conjugates can be exported from animal cells by putative membrane ATP-dependent pump systems [3] after which they are metabolized via the mercapturate pathway and eventually eliminated. An extraordinary feature of the glutathione S-transferase superfamily is the occurrence of multiple enzyme forms that, according to sequence similarities and subc...

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“…However, no soluble GST activity towards microsomally activated AFB1 has been found in liver cytosol from one-month old male turkeys (Klein et al, 2000), a finding that was later confirmed in male turkeys 9, 41, and 65 days of age (Klein et al, 2002). GSTs from the liver of one-day-old chicks (Chang et al, 1990) and nucleotide sequences of Alpha-class (Liu et al, 1993), Mu-class (Liu & Tam, 1991), Theta-class (Hsiao et al, 1995) and Sigma-class (Thomson et al, 1998) GSTs from chicken liver have been characterized, but there are no reports for their role in AFBO trapping with GSH. The role of other conjugation reactions on AFB1 metabolism in poultry is still uncertain.…”

Section: Trapping and Conjugation Of Aflatoxin B1 Metabolites In Commmentioning

confidence: 98%

Biotransformation of Aflatoxin B1 and Its Relationship with the Differential Toxicological Response to Aflatoxin in Commercial Poultry Species

Díaz¹,

Murcia²

2011

Aflatoxins - Biochemistry and Molecular Biology

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Nucleotide sequence of a class μ glutathione S-transferase from chicken liver

Cited by 28 publications

References 13 publications

Glutathione S-transferases in the Japanese quail: Tissue distribution and purification of the liver isozymes

Glutathione S-transferases in the Japanese quail: Tissue distribution and purification of the liver isozymes

X‐ray crystal structures of cytosolic glutathione S‐transferases

Biotransformation of Aflatoxin B1 and Its Relationship with the Differential Toxicological Response to Aflatoxin in Commercial Poultry Species

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