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Sökning: WFRF:(Mannervik B )

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  • Cameron, AD, et al. (författare)
  • Crystal structure of human glyoxalase .1. Evidence for gene duplication and 3D domain swapping
  • 1997
  • Ingår i: EMBO JOURNAL. - : OXFORD UNIV PRESS. - 0261-4189. ; 16:12, s. 3386-3395
  • Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
    • The zinc metalloenzyme glyoxalase I catalyses the glutathione-dependent inactivation of toxic methylglyoxal. The structure of the dimeric human enzyme in complex with S-benzyl-glutathione has been determined by multiple isomorphous replacement (MIR) and r
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  • Cameron, AD, et al. (författare)
  • Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue
  • 1999
  • Ingår i: STRUCTURE WITH FOLDING & DESIGN. - : CURRENT BIOLOGY LTD. - 0969-2126. ; 7:9, s. 1067-1078
  • Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
    • Background: Glyoxalase II, the second of two enzymes in the glyoxalase system, is a thiolesterase that catalyses the hydrolysis of S-D-lactoylgtutathione to form glutathione and D-lactic acid. Results: The structure of human glyoxalase II was solved initi
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  • Dahl, Niklas, et al. (författare)
  • Missense mutations in the human glutathione synthetase gene result in severe metabolic acidosis, 5-oxoprolinuria, hemolytic anemia and neurological dysfunction
  • 1997
  • Ingår i: Human Molecular Genetics. - : Oxford University Press (OUP). - 0964-6906 .- 1460-2083. ; 6:7, s. 1147-1152
  • Tidskriftsartikel (refereegranskat)abstract
    • Severe glutathione synthetase (GS) deficiency is a rare genetic disorder with neonatal onset. The enzymatic block of the gamma-glutamyl cycle leads to a generalized glutathione deficiency. Clinically affected patients present with severe metabolic acidosis, 5-oxoprolinuria, increased rate of hemolysis and defective function of the central nervous system. The disorder is inherited in an autosomal recessive mode and, until recently, the molecular basis has remained unknown. We have sequenced 18 GS alleles associated with enzyme deficiency and we detected missense mutations by direct sequencing of cDNAs and genomic DNA. In total, 13 different mutations were identified. Four patients were found to be compound heterozygotes and two individuals were apparently homozygous. Reduced enzymatic activities were demonstrated in recombinant protein expressed from cDNAs in four cases with different missense mutations. The results from biochemical analysis of patient specimens, supported by the properties of the expressed mutant proteins, indicate that a residual activity is present in affected individuals. Our results suggest that complete loss of function of both GS alleles is probably lethal. It is postulated that missense mutations will account for the phenotype in the majority of patients with severe GS deficiency.
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  • Dragani, B, et al. (författare)
  • Role of conserved local motifs in folding and stability of hGSTP1-1
  • 2001
  • Ingår i: CHEMICO-BIOLOGICAL INTERACTIONS. - : ELSEVIER SCI IRELAND LTD. - 0009-2797. ; 133:1-3, s. 17-18
  • Tidskriftsartikel (refereegranskat)abstract
    • We investigated, by site directed mutagenesis, the role played by a conserved N-capping box and hydrophobic staple motif in the folding and stability of human GSTPl-1. The corresponding mutants, I149A, S150A, D153A and Y154A, in which these motifs have be
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  • Mannervik, B, et al. (författare)
  • An evolutionary approach to the design of glutathione-linked enzymes
  • 1998
  • Ingår i: CHEMICO-BIOLOGICAL INTERACTIONS. - : ELSEVIER SCI IRELAND LTD. - 0009-2797. ; 112, s. 15-21
  • Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
    • Studies of protein structure provide information about principles of protein design that have come into play in natural evolution. This information can be exploited in the redesign of enzymes for novel functions. The glutathione-binding domain of glutathi
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  • Sinning, I, et al. (författare)
  • Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes.
  • 1993
  • Ingår i: J Mol Biol. - 0022-2836. ; 232:1, s. 192-212
  • Tidskriftsartikel (refereegranskat)abstract
    • The crystal structure of human alpha class glutathione transferase A1-1 has been determined and refined to a resolution of 2.6 A. There are two copies of the dimeric enzyme in the asymmetric unit. Each monomer is built from two domains. A bound inhibitor, S-benzyl-glutathione, is primarily associated with one of these domains via a network of hydrogen bonds and salt-links. In particular, the sulphur atom of the inhibitor forms a hydrogen bond to the hydroxyl group of Tyr9 and the guanido group of Arg15. The benzyl group of the inhibitor is completely buried in a hydrophobic pocket. The structure shows an overall similarity to the mu and pi class enzymes particularly in the glutathione-binding domain". The main difference concerns the extended C terminus of the alpha class enzyme which forms an extra alpha-helix that blocks one entrance to the active site and makes up part of the substrate binding site.
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  • Andersson, C, et al. (författare)
  • Activation and inhibition of microsomal glutathione transferase from mouse liver.
  • 1988
  • Ingår i: Biochemical Journal. - 0264-6021 .- 1470-8728. ; 249:3, s. 819-23
  • Tidskriftsartikel (refereegranskat)abstract
    • Mouse liver microsomal glutathione transferase was purified in an N-ethylmaleimide-activated as well as an unactivated form. The enzyme had a molecular mass of 17 kDa and a pI of 8.8. It showed cross-reactivity with antibodies raised against rat liver microsomal glutathione transferase, but not with any of the available antisera raised against cytosolic glutathione transferases. The fully N-ethylmaleimide-activated enzyme could be further activated 1.5-fold by inclusion of 1 microM-bromosulphophthalein in the assay system. The latter effect was reversible, which was not the case for the N-ethylmaleimide activation. At 20 microM-bromosulphophthalein the activated microsomal glutathione transferase was strongly inhibited, while the unactivated form was activated 2.5-fold. Inhibitors of the microsomal glutathione transferase from mouse liver showed either about the same I50 values for the activated and the unactivated form of the enzyme, or significantly lower I50 values for the activated form compared with the unactivated form. The low I50 values and the steep slope of the activity-versus-inhibitor-concentration curves for the latter group of inhibitors tested on the activated enzyme indicate a co-operative effect involving conversion of activated enzyme into the unactivated form, as well as conventional inhibition of the enzyme.
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  • BJORNESTEDT, R, et al. (författare)
  • FUNCTIONAL-SIGNIFICANCE OF ARGININE-15 IN THE ACTIVE-SITE OF HUMAN CLASS-ALPHA GLUTATHIONE TRANSFERASE A1-1
  • 1995
  • Ingår i: JOURNAL OF MOLECULAR BIOLOGY. - : ACADEMIC PRESS (LONDON) LTD. - 0022-2836. ; 247:4, s. 765-773
  • Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
    • Arg15 is a conserved active-site residue in class Alpha glutathione transferases. X-ray diffraction studies of human glutathione transferase Al-1 have shown that N-epsilon of this amino acid residue is adjacent to the sulfur atom of a glutathione derivati
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  • Frickel, EM, et al. (författare)
  • Yeast glyoxalase I is a monomeric enzyme with two active sites
  • 2001
  • Ingår i: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 276:3, s. 1845-1849
  • Tidskriftsartikel (refereegranskat)abstract
    • The tertiary structure of the monomeric yeast glyoxalase I has been modeled based on the crystal structure of the dimeric human glyoxalase I and a sequence alignment of the two enzymes, The model suggests that yeast glyoxalase I has two active sites conta
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  • Gardner, JL, et al. (författare)
  • Characterization of a peptide antibody toward hGSTA4-4
  • 2001
  • Ingår i: CHEMICO-BIOLOGICAL INTERACTIONS. - : ELSEVIER SCI IRELAND LTD. - 0009-2797. ; 133:1-3, s. 63-67
  • Tidskriftsartikel (refereegranskat)abstract
    • A polyclonal antibody was developed that can discriminate human alpha class glutathionetransferase 4-4 (hGSTA4-4). This was accomplished by first determining candidate peptide sequences of the hGSTA4 subunit, which exhibited low homology to other human GS
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  • Hubert, Shawna M., et al. (författare)
  • Conservation of Glutathione Transferase mRNA and Protein Sequences Similar to Human and Horse Alpha Class GST A3-3 across Dog, Goat, and Opossum Species
  • 2023
  • Ingår i: Biomolecules. - 2218-273X. ; 13:9
  • Tidskriftsartikel (refereegranskat)abstract
    • The glutathione transferase A3-3 (GST A3-3) homodimeric enzyme is the most efficient enzyme that catalyzes isomerization of the precursors of testosterone, estradiol, and progesterone in the gonads of humans and horses. However, the presence of GST A3-3 orthologs with equally high ketosteroid isomerase activity has not been verified in other mammalian species, even though pig and cattle homologs have been cloned and studied. Identifying GSTA3 genes is a challenge because of multiple GSTA gene duplications (e.g., 12 in the human genome); consequently, the GSTA3 gene is not annotated in most genomes. To improve our understanding of GSTA3 gene products and their functions across diverse mammalian species, we cloned homologs of the horse and human GSTA3 mRNAs from the testes of a dog, goat, and gray short-tailed opossum, the genomes of which all currently lack GSTA3 gene annotations. The resultant novel GSTA3 mRNA and inferred protein sequences had a high level of conservation with human GSTA3 mRNA and protein sequences (≥70% and ≥64% identities, respectively). Sequence conservation was also apparent for the 12 residues of the “H-site” in the 222 amino acid GSTA3 protein that is known to interact with the steroid substrates. Modeling predicted that the dog GSTA3-3 may be a more active ketosteroid isomerase than the corresponding goat or opossum enzymes. However, expression of the GSTA3 gene was higher in liver than in other dog tissue. Our results improve understanding of the active sites of mammalian GST A3-3 enzymes, inhibitors of which might be useful for reducing steroidogenesis for medical purposes, such as fertility control or treatment of steroid-dependent diseases.
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  • Hurst, R, et al. (författare)
  • Phospholipid hydroperoxide glutathione peroxidase activity of human glutathione transferases
  • 1998
  • Ingår i: BIOCHEMICAL JOURNAL. - : PORTLAND PRESS. ; 332
  • Annan publikation (övrigt vetenskapligt/konstnärligt)abstract
    • Human glutathione transferases (GSTs) from Alpha (A), Mu (M) and Theta (T) classes exhibited glutathione peroxidase activity towards phospholipid hydroperoxide. The specific activities are in the order: GST A1-1 > GST T1-1 > GST M1-1 > GST A2-2 > GST A4-
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  • Jemth, P, et al. (författare)
  • Ser11 plays several roles in the catalytic mechanism of rat glutathione transferase T2-2
  • 2001
  • Ingår i: CHEMICO-BIOLOGICAL INTERACTIONS. - : ELSEVIER SCI IRELAND LTD. - 0009-2797. ; 133:1-3, s. 178-181
  • Tidskriftsartikel (refereegranskat)abstract
    • Ser11 in rat glutathione transferase T2-2 promotes several steps in the catalyzed reaction pathway of the enzyme. First, the residue lowers the pK(a) value of the enzyme-bound glutathione thiol by 2.2 pH units, from 7.9 to 5.7. Secondly, the presence of S
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  • Lien, S, et al. (författare)
  • Human glutathione transferase Al-1 demonstrates both half-of-the-sites and all-of-the-sites reactivity
  • 2001
  • Ingår i: JOURNAL OF BIOLOGICAL CHEMISTRY. - : AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC. - 0021-9258. ; 276:38, s. 35599-35605
  • Tidskriftsartikel (refereegranskat)abstract
    • A study of the kinetics of a heterodimeric variant of glutathione transferase (GST) A1-1 has led to the conclusion that, although the wild-type enzyme displays all-of-the-sites reactivity in nucleophilic aromatic substitution reactions, it demonstrates ha
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  • Resultat 1-50 av 71

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