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

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

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

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).

An Amino Acid Residue (S201) in the Retinal Binding Pocket Regulates the Photoreaction Pathway of Phoborhodopsin

Biochemistry ◽  
2011 ◽  
Vol 50 (33) ◽  
pp. 7177-7183 ◽  
Author(s):  
Gang Dai ◽  
Yu Zhang ◽  
Jun Tamogami ◽  
Makoto Demura ◽  
Naoki Kamo ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Binding Pocket ◽  
Retinal Binding Pocket

scholarly journals Endocrine Disruption: Structural Interactions of Androgen Receptor against Di(2-ethylhexyl) Phthalate and Its Metabolites

Toxics ◽  
2020 ◽  
Vol 8 (4) ◽  
pp. 115
Author(s):  
Mohd Amin Beg ◽  
Ishfaq Ahmad Sheikh
Keyword(s):  
Hydrogen Bonding ◽  
Androgen Receptor ◽  
Amino Acid ◽  
Amino Acid Residue ◽  
Parent Compound ◽  
Binding Pocket ◽  
Primary Metabolite ◽  
Binding Data ◽  
Available Information ◽  
Ethylhexyl Phthalate

Diethylhexyl phthalate (DEHP) is a commonly used plasticizer in the manufacture of polyvinyl chloride plastics for household and commercial use. DEHP is a ubiquitous ecocontaminant and causes developmental and reproductive problems in children and adults. After exposure, DEHP is metabolized by endogenous hydrolysis and oxidation into the primary metabolite, mono-(2-ethylhexyl) phthalate (MEHP), and the secondary metabolites, mono-(2-ethyl-5-hydroxhexyl)phthalate (5-OH-MEHP), mono-(2-ethyl-5-oxohexyl) phthalate (5-oxo-MEHP), mono-(2-ethyl-5-carboxypentyl) phthalate (5-cx-MEPP), and mono-[(2-carboxymethyl)hexyl] phthalate (2-cx-MMHP). Very few studies have been reported on the adverse effects of DEHP metabolites, and the available information indicates that the metabolites might also be equally or more active as compared to the parent compound. In the present study, induced fit docking was used for structural binding characterization of the above five DEHP metabolites with androgen receptor (AR) to predict the potential endocrine-disrupting effects of these metabolites in AR signaling. All the DEHP metabolites interacted with the ligand-binding pocket of AR forming amino-acid residue interactions, hydrogen bonding, and pi-pi interactions. The binding energy of DEHP with AR was similar to that of native ligand testosterone. The amino-acid residue interactions of DEHP metabolites had 91–100% similarity compared to that of testosterone. In addition, all the DEHP metabolites and testosterone showed a common hydrogen bonding interaction with amino-acid Arg-752 of AR. Taken together, the structural binding data in the present study suggested the potential for DEHP metabolites to disrupt AR signaling, which may lead to androgen-related reproductive dysfunction.

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