Contribution of amino acid residue 208 in the hydrophobic binding site to the catalytic mechanism of human glutathione transferase A1-1

Biochemistry ◽  
1994 ◽  
Vol 33 (39) ◽  
pp. 11717-11723 ◽  
Author(s):  
Mikael Widersten ◽  
Robert Bjoernestedt ◽  
Bengt Mannervik
Keyword(s):  
Amino Acid ◽  
Binding Site ◽  
Amino Acid Residue ◽  
Catalytic Mechanism ◽  
Glutathione Transferase ◽  
Hydrophobic Binding

scholarly journals Irreversible site-directed labeling of the 4-aminobutyrate binding site by tritiated meta-sulfonate benzene diazonium . Contribution of a nucleophilic amino acid residue of the alpha1 subunit

1999 ◽  
Vol 265 (1) ◽  
pp. 189-194 ◽  
Author(s):  
Patrice Jacques ◽  
Philippe Perret ◽  
Marie-Jeanne Bouchet ◽  
Bernard Foucaud ◽  
Maurice Goeldner ◽  
...  
Keyword(s):  
Amino Acid ◽  
Binding Site ◽  
Amino Acid Residue ◽  
Benzene Diazonium

Tetranectin-Binding Site on Plasminogen Kringle 4 Involves the Lysine-Binding Pocket and at Least One Additional Amino Acid Residue†

Biochemistry ◽  
2000 ◽  
Vol 39 (25) ◽  
pp. 7414-7419 ◽  
Author(s):  
Jonas H. Graversen ◽  
Bent W. Sigurskjold ◽  
Hans C. Thøgersen ◽  
Michael Etzerodt
Keyword(s):  
Amino Acid ◽  
Binding Site ◽  
Amino Acid Residue ◽  
Binding Pocket ◽  
Additional Amino Acid

Identification of an amino acid residue involved in the substrate-binding site of rat liver uricase by site-directed mutagenesis

1992 ◽  
Vol 187 (1) ◽  
pp. 101-107 ◽  
Author(s):  
Masaki Ito ◽  
Seiya Kato ◽  
Masamichi Nakamura ◽  
Go Mitiko ◽  
Yasuyuki Takagi
Keyword(s):  
Amino Acid ◽  
Binding Site ◽  
Rat Liver ◽  
Amino Acid Residue ◽  
Substrate Binding ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Substrate Binding Site

scholarly journals Hemoglobin Okayama [β-2 (NA 2) His → Gln]: A new ‘silent’ hemoglobin variant with substituted amino acid residue at the 2,3-diphosphoglycerate binding site

FEBS Letters ◽  
1983 ◽  
Vol 156 (1) ◽  
pp. 20-22 ◽  
Author(s):  
Teruo Harano ◽  
Keiko Harano ◽  
Susumu Shibata ◽  
Satoshi Ueda ◽  
Hiroo Mori ◽  
...  
Keyword(s):  
Amino Acid ◽  
Binding Site ◽  
Amino Acid Residue ◽  
Hemoglobin Variant

Amino acid residue 200 on the α1 subunit of GABAA receptors affects the interaction with selected benzodiazepine binding site ligands

1998 ◽  
Vol 354 (2-3) ◽  
pp. 283-287 ◽  
Author(s):  
Martin T. Schaerer ◽  
Andreas Buhr ◽  
Roland Baur ◽  
Erwin Sigel
Keyword(s):  
Amino Acid ◽  
Binding Site ◽  
Amino Acid Residue ◽  
Gabaa Receptors ◽  
Benzodiazepine Binding ◽  
Α1 Subunit

Mapping the active site of papain with the aid of peptide substrates and inhibitors

1970 ◽  
Vol 257 (813) ◽  
pp. 249-264 ◽  
Keyword(s):  
Amino Acid ◽  
Binding Site ◽  
Amino Acid Residue ◽  
Active Site ◽  
Proteolytic Enzymes ◽  
Reaction Rates ◽  
Side Chain ◽  
Peptide Substrates ◽  
Methyl Group ◽  
Kinetics Of

The active site of an enzyme performs the twofold function of binding a substrate and catalysing a reaction. The efficiency of these actions determines the overall activity of the enzyme towards the particular substrate, i.e. determines the specificity of the enzyme. It is therefore possible to obtain information on the active site by the kinetics of the enzyme’s reactions with different substrates and inhibitors. An important feature of the active site is its size. It should be possible to 'measure’ this by using substrates or inhibitors large enough to show up the interactions of the furthermost parts of the binding site. In the present series of investigations on proteolytic enzymes, our approach is to compare the activity of the enzyme towards ( a ) peptides of increasing length, ( b ) diastereoisomeric pairs of peptides in which a particular amino acid residue has been replaced by its antipode, and ( c ) pairs of substrates in which a particular side chain (say a methyl group) has been replaced by another (say an aromatic group). The influence of these changes on reaction rates as a function of distance from the point of cleavage indicates the extent of the active site (Schechter, Abramowitz & Berger 1965; Abramowitz, Schechter & Berger 1967).

Characterization of Met-139 as the photolabeled amino acid residue in the steroid binding site of sex hormone binding globulin using .DELTA.6 derivatives of either testosterone or estradiol as unsubstituted photoaffinity labeling reagents

Biochemistry ◽  
1992 ◽  
Vol 31 (33) ◽  
pp. 7609-7621 ◽  
Author(s):  
Catherine Grenot ◽  
Arnaud De Montard ◽  
Thierry Blachere ◽  
Marc Rolland De Ravel ◽  
Elisabeth Mappus ◽  
...  
Keyword(s):  
Amino Acid ◽  
Binding Site ◽  
Amino Acid Residue ◽  
Photoaffinity Labeling ◽  
Sex Hormone ◽  
Sex Hormone Binding Globulin ◽  
Hormone Binding ◽  
Steroid Binding ◽  
Derivatives Of

The 5-ketofructose reductase of Gluconobacter sp. strain CHM43 is a novel class in the shikimate dehydrogenase family

2021 ◽  
Author(s):  
Thuy Minh Nguyen ◽  
Masaru Goto ◽  
Shohei Noda ◽  
Minenosuke Matsutani ◽  
Yuki Hodoya ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Binding Site ◽  
Catalytic Mechanism ◽  
Substrate Binding ◽  
High Yield ◽  
Strong Increase ◽  
Amino Acid Residues ◽  
Shikimate Dehydrogenase ◽  
Substrate Binding Site

Gluconobacter sp. CHM43 oxidizes mannitol to fructose and then does fructose to 5-keto-D-fructose (5KF) in the periplasmic space. Since NADPH-dependent 5KF reductase was found in the soluble fraction of Gluconobacter spp., 5KF might be transported into the cytoplasm and metabolized. Here we identified the GLF_2050 gene as the kfr gene encoding 5KF reductase (KFR). A mutant strain devoid of the kfr gene showed lower KFR activity and no 5KF consumption. The crystal structure revealed that KFR is similar to NADP + -dependent shikimate dehydrogenase (SDH), which catalyzes the reversible NADP + -dependent oxidation of shikimate to 3-dehydroshikimate. We found that several amino acid residues in the putative substrate-binding site of KFR were different from those of SDH. Phylogenetic analyses revealed that only a subclass in the SDH family containing KFR conserved such a unique substrate-binding site. We constructed KFR derivatives with amino acid substitutions, including replacement of Asn21 in the substrate-binding site with Ser that is found in SDH. The KFR-N21S derivative showed a strong increase in the K M value for 5KF, but a higher shikimate oxidation activity than wild-type KFR, suggesting that Asn21 is important for 5KF binding. In addition, the conserved catalytic dyad Lys72 and Asp108 were individually substituted for Asn. The K72N and D108N derivatives showed only negligible activities without a dramatic change in the K M value for 5KF, suggesting a similar catalytic mechanism to that of SDH. Taken together, we suggest that KFR is a new member of the SDH family. Importance A limited number of species of acetic acid bacteria, such as Gluconobacter sp. strain CHM43, produce 5-ketofructose at a high yield, a potential low calorie sweetener. Here we show that an NADPH-dependent 5-ketofructose reductase (KFR) is involved in 5-ketofructose degradation and we characterize this enzyme with respect to its structure, phylogeny, and function. The crystal structure of KFR was similar to that of shikimate dehydrogenase, which is functionally crucial in the shikimate pathway in bacteria and plants. Phylogenetic analysis suggested that KFR is positioned in a small sub-group of the shikimate dehydrogenase family. Catalytically important amino acid residues were also conserved and their relevance was experimentally validated. Thus, we propose KFR as a new member of shikimate dehydrogenase family.

Sign in / Sign up

Export Citation Format

Share Document