Donor substrate specificity of bovine kidney gamma-glutamyltransferase

Agblor, Anita A.; Josephy, P. David

doi:10.1016/j.cbi.2013.02.007

Cited by 4 publications

(2 citation statements)

References 76 publications

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“…An investigation of the rates of transpeptidation of a series of donor GSH S-conjugates of aromatic compounds showed that the catalytic efficiency varied by a factor of four with bovine kidney GGT (Agblor and Josephy 2013). The GSH analog ophthalmic acid (L-c-Glu-L-a-aminobutyryl-Gly) and several S-substituted GSH analogs also serve as donor substrates for rat kidney GGT (Tate and Meister 1974a); GSSG and c-(DL-a-methylglutamyl)-L-Cys-Gly are poor donor substrates with Met as the acceptor.…”

Section: Transpeptidationmentioning

confidence: 99%

The mercapturic acid pathway

Hanna

Anders

2019

Critical Reviews in Toxicology

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The mercapturic acid pathway is a major route for the biotransformation of xenobiotic and endobiotic electrophilic compounds and their metabolites. Mercapturic acids (N-acetyl-L-cysteine S-conjugates) are formed by the sequential action of the glutathione transferases, c-glutamyltransferases, dipeptidases, and cysteine S-conjugate N-acetyltransferase to yield glutathione S-conjugates, L-cysteinylglycine S-conjugates, L-cysteine S-conjugates, and mercapturic acids; these metabolites constitute a "mercapturomic" profile. Aminoacylases catalyze the hydrolysis of mercapturic acids to form cysteine S-conjugates. Several renal transport systems facilitate the urinary elimination of mercapturic acids; urinary mercapturic acids may serve as biomarkers for exposure to chemicals. Although mercapturic acid formation and elimination is a detoxication reaction, L-cysteine S-conjugates may undergo bioactivation by cysteine Sconjugate b-lyase. Moreover, some L-cysteine S-conjugates, particularly L-cysteinyl-leukotrienes, exert significant pathophysiological effects. Finally, some enzymes of the mercapturic acid pathway are described as the so-called "moonlighting proteins," catalytic proteins that exert multiple biochemical or biophysical functions apart from catalysis.

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Section: Transpeptidationmentioning

confidence: 99%

The mercapturic acid pathway

Hanna

Anders

2019

Critical Reviews in Toxicology

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“…Because many sensitive methods are available for the accurate quantification of amino acids, as reviewed in [23], this approach would enable quantification of low concentrations of GSHconjugates provided that hydrolysis to glutamic acid and glycine is quantitative and that these amino acids are not further degraded under the conditions used. Hydrolysis of GSH-conjugates can be done non-enzymatically by acidic or alkaline hydrolysis [23] or using ␥-glutamyltranspeptidase and dipeptidases [24,25]. In the present study alkaline hydrolysis was applied followed by subsequently derivatization by o-phthaldialdehyde/N-acetylcysteine (OPA/NAC), a well-established and highly sensitive method for fluorimetric quantification of amino acids [23,26].…”

Section: Introductionmentioning

confidence: 99%

Generic method for the absolute quantification of glutathione S-conjugates: Application to the conjugates of acetaminophen, clozapine and diclofenac

Braver

Vermeulen

Commandeur

2017

Journal of Chromatography B

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γ-Glutamyl transpeptidase (GgtA) of Aspergillus nidulans is not necessary for bulk degradation of glutathione

et al. 2014

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Aspergillus nidulans exhibited high γ-glutamyl transpeptidase (γGT) activity in both carbon-starved and carbon-limited cultures. Glucose repressed, but casein peptone increased γGT production. Null mutation of creA did not influence γGT formation, but the functional meaB was necessary for the γGT induction. Deletion of the AN10444 gene (ggtA) completely eliminated the γGT activity, and the mRNA levels of ggtA showed strong correlation with the observed γGT activities. While ggtA does not contain a canonical signal sequence, the γGT activity was detectable both in the fermentation broth and in the hyphae. Deletion of the ggtA gene did not prevent the depletion of glutathione observed in carbon-starved and carbon-limited cultures. Addition of casein peptone to carbon-starved cultures lowered the formation of reactive species (RS). Deletion of ggtA could hinder this decrease and resulted in elevated RS formation. This effect of γGT on redox homeostasis may explain the reduced cleistothecia formation of ΔggtA strains in surface cultures.

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Donor substrate specificity of bovine kidney gamma-glutamyltransferase

Cited by 4 publications

References 76 publications

The mercapturic acid pathway

The mercapturic acid pathway

Generic method for the absolute quantification of glutathione S-conjugates: Application to the conjugates of acetaminophen, clozapine and diclofenac

γ-Glutamyl transpeptidase (GgtA) of Aspergillus nidulans is not necessary for bulk degradation of glutathione

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