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Topic: Allosteric site


In the News (Sun 27 May 12)

  
  Allosteric regulation - Wikipedia, the free encyclopedia
In biochemistry, allosteric regulation is the regulation of an enzyme or protein by binding an effector molecule at the protein's allosteric site (that is, a site other than the protein's active site).
Allosteric activation, such as the binding of oxygen molecules to hemoglobin, occurs when the binding of one ligand enhances the attraction between substrate molecules and other binding sites.
Many allosteric proteins are regulated by their substrate; such a substrate is considered a homotropic allosteric modulator, and is typically an activator.
en.wikipedia.org /wiki/Allosteric_modulation   (629 words)

  
 [No title]
Note that the binding site of PGC in the T state overlaps the allosteric binding site of ADP in the R state ("ADP-allo") and hence their binding is mutually exclusive.
Note that the active site is located at the interface between two subunits and that the allosteric site interacts directly with the adjacent active site.
The phosphate group of PGC binds to the allosteric site in the T state in very nearly the same position that the beta phosphate group of "ADP-allo" binds to the R state allosteric site; both phosphate groups bind to the side chains of the same three Arg residues (not shown).
www.usd.edu /~bnoiva/13-pfk.txt   (1291 words)

  
 Molecular Interactions in Cell Events: Catalysis : Control of enzyme activity : Allosteric enzymes
Allosteric enzymes change their conformation in response to the binding of a regulating molecule.
Allosteric enzymes have two conformations, one that is active, catalytically, and the other that is inactive.
Negative modulators (inhibitors) bind to an allosteric site that stabilises the inactive conformation of the molecule.
scholar.hw.ac.uk /site/biology/topic11.asp?outline=   (202 words)

  
 Penn State Faculty Research Expertise Database (FRED)   (Site not responding. Last check: 2007-10-09)
Allosteric site on muscarinic acetylcholine receptors: a single amino acid in transmembrane region 7 is critical to the subtype selectivities of caracurine V derivatives and alkane-bisammonium ligands.
Mohr K. Ellis J. Allosteric site on muscarinic acetylcholine receptors: a single amino acid in transmembrane region 7 is critical to the subtype selectivities of caracurine V derivatives and alkane-bisammonium ligands.
These allosteric ligands included two alkane-bisammonium compounds and a series of caracurine V derivatives, which are structurally closely related to (but stereochemically different from) the prototype allosteric ligand alcuronium.
fred.hmc.psu.edu /ds/retrieve/fred/publication/11752217   (320 words)

  
 [No title]   (Site not responding. Last check: 2007-10-09)
The allosteric enzyme is a dimer with identical subunits so it is called a homodimer (A-A, where 'A' represents one of the identical subunits).
The binding sites for the allosteric modifier are shown as being remote from the active site.
Thus, the influence of the allosteric modifier must be transmitted through the framework of the enzyme in order to influence the activity of the enzyme - either positively or negatively.
www.bio.mtu.edu /campbell/401lec17p2.html   (634 words)

  
 Answer Key for Re   (Site not responding. Last check: 2007-10-09)
In allosteric regulation, a metabolic pathway is controlled by an allosteric enzyme, which is normally an enzyme that catalyzes a reaction in the initial parts of a pathway.
An allosteric enzyme has at least one allosteric site, which is a site apart from the active site, to which the allosteric regulator bonds reversibly.
When the allosteric regulator is present in the allosteric site, the enzyme will either be in its active conformation or its inactive conformation, depending on whether the regulator is an inhibitor or an activator.
www2.tltc.ttu.edu /dini/key2b(1403)00.htm   (652 words)

  
 Enzyme Regulation
Effectors bind to a specific site on the enzyme called the allosteric site (allo means "other than", the allosteric site is a site "other than" the active site).
Typically, the allosteric site is a site on the enzyme that is remote from the active site.
Allosteric regulation is achieved through noncovalent interactions (binding) of substrates and effectors to the enzyme.
www.people.virginia.edu /~rjh9u/IntroBio/bio201/lectures/Lecture14.html   (456 words)

  
 Are the Common Allosteric Models Correct?
For our purposes, allosteric refers to the regulation (either inhibition or activation) of enzyme activity due to the binding of a metabolite to a site on the enzyme that is different from the active site.
An allosteric inhibitor binds to an allosteric site and shifts the conformational equilibrium to one that is relatively inactive.
The purpose of the experiment is to determine if the individual allosteric sites (x-axis) have an effect on the bonding of a specific active site.
www.angelfire.com /falcon/cheesehead/reinhart.html   (852 words)

  
 Regulation of Metabolism
However, when the allosteric site is occupied by the effector molecule, the configuration of the active site is changed so that it is now unable to recognize and bind to its substrate (Figure 1).
The effector molecule of certain allosteric enzymes binds to its allosteric site and consequently transforms the enzyme from an inactive to an active state (Figure 2).
Tryptophan is the effector molecule for allosteric enzyme a.
textbookofbacteriology.net /regulation.html   (3878 words)

  
 Allosteric Site on Muscarinic Acetylcholine Receptors: A Single Amino Acid in Transmembrane Region 7 Is Critical to the ...   (Site not responding. Last check: 2007-10-09)
Allosteric Site on Muscarinic Acetylcholine Receptors: A Single Amino Acid in Transmembrane Region 7 Is Critical to the Subtype Selectivities of Caracurine V Derivatives and Alkane-Bisammonium Ligands -- Buller et al.
of the allosteric ligand at the NMS-occupied receptor (Lazareno
for allosteric ligands at the free and NMS-liganded receptors
molpharm.aspetjournals.org /cgi/content/full/61/1/160   (4649 words)

  
 Allosteric Regulation of Catalytic Activity: Escherichia coli Aspartate Transcarbamoylase versus Yeast Chorismate ...
The residues which change their position during allosteric transition and thereby transduce the signal of effector binding from the allosteric to the active site are shown as stick models (green, carbon; blue, nitrogen; red, oxygen).
The position of the catalytic site inhibitor in the T and R state is derived from a superposition with the super R state structure using residues 1 to 214 and 224 to 254.
Carbamyl phosphate: an allosteric substrate for aspartate transcarbamylase of Escherichia coli.
mmbr.asm.org /cgi/content/full/65/3/404   (10340 words)

  
 Search Results for allosteric site - Encyclopædia Britannica
Allosteric control can operate in many ways; two examples serve to illustrate some general effects.
Mixtures of myosin and actin are used in the test tube to study the relationship between the ATP breakdown reaction and the interaction of myosin and actin.
A biosynthetic pathway is usually controlled by an allosteric effector produced as the end product of that pathway, and the pacemaker enzyme on which the effector acts usually catalyzes the first...
www.britannica.com /search?query=allosteric+site   (566 words)

  
 Metabolism
A group of enzymes known as allosteric enzymes have two binding sites: (1) a substrate binding site (the active site) and (2) a cofactor binding site (the allosteric site).
In these enzymes the binding of the cofactor to the allosteric site will change the conformation of the enzyme.
Thus the activity of allosteric enzymes is controlled by the concentration of cofactors.
www2.hawaii.edu /~johnb/micro/medmicro/medmicro.4.html   (544 words)

  
 G Protein-Coupled Receptor Allosterism and Complexing -- Christopoulos and Kenakin 54 (2): 323 -- Pharmacological ...
the binding of the substrate to the isosteric site, and vice versa.
Ligand A binds to the orthosteric site, whereas ligand B, the allosteric modulator, binds to the allosteric site.
Allosteric ligand-mediated receptor-G protein interactions are not restricted to the muscarinic acetylcholine receptors.
pharmrev.aspetjournals.org /cgi/content/full/54/2/323   (8874 words)

  
 index   (Site not responding. Last check: 2007-10-09)
Allosteric regulation is the regulation of an enzyme or protein by the binding of an effector molecule at the protein's allosteric site.
An allosteric inhibitor binds to an allosteric site (one other than the active site) and shifts the conformational equillibrium to one that is relatively inactive.
In his research, he has challenged the two common allosteric models that are prevalent in research in the field today.
www.geocities.com /bich107group1   (117 words)

  
 Synthesis of AMP analogs and their use for studies on the allosteric site of rabbit muscle glycogen phosphorylase b -- ...
Synthesis of AMP analogs and their use for studies on the allosteric site of rabbit muscle glycogen phosphorylase b -- Eguchi et al.
Synthesis of AMP analogs and their use for studies on the allosteric site of rabbit muscle glycogen phosphorylase b
The nature of the allosteric site of phosphorylase b is discussed based on
jb.oupjournals.org /cgi/content/abstract/81/5/1401   (222 words)

  
 MOLECULAR BIOLOGY: ALLOSTERIC REGULATION OF RNA
An important mechanism for controlling protein activity is allosteric regulation by a small molecule (i.e., binding of a small molecule to the protein at a location remote from the active site).
Binding of this regulatory compound to the allosteric site induces structural rearrangements in the protein that are relayed to the active site, which then becomes either stable or unstable.
In allosteric proteins, multiple subunits act cooperatively: Once a regulator is bound to one subunit, another subunit responds with dramatically enhanced affinity, allowing the protein's activity to be modulated as a function of slight changes in the regulator's concentration.
scienceweek.com /2004/sc041119-1.htm   (1615 words)

  
 Combined Allosteric and Competitive Interaction between Extracellular Na+ and K+ During Ion Transport by the alpha 1, ...
Combined Allosteric and Competitive Interaction between Extracellular Na+ and K+ During Ion Transport by the alpha 1, alpha 2, and alpha 3 Isoforms of the Na, K-ATPase -- Balshaw et al.
The affinity for the allosteric site in the rat
that the occupation of the allosteric site increased the affinity
www.biophysj.org /cgi/content/full/79/2/853   (4661 words)

  
 Cell Biology Terms   (Site not responding. Last check: 2007-10-09)
This may result in a conformational change at the active site so that the normal substrate cannot bind to it.
The allosteric property is useful in the regulation of enzyme activity.
A regulatory enzyme whose activity is modified by the noncovalent binding of a particular metabolite at a site (the allosteric site) other than the active site.
www.mdstud.chalmers.se /~vivi/interests/biodict.html   (427 words)

  
 Biology
An allosteric site is a specific receptor site on an enzyme molecule remote from the active site.
Molecules tend to bind to the allosteric site and change the shape of the active site making them either more or less receptive to the substrate.
A competitive inhibitor is a substance that reduces the activity of an enzyme by entering the active site in place of the substrate whose structure it mimics.
www.msu.edu /~browerst/ChSevenVoc.html   (517 words)

  
 ALLOSTERIC SITE   (Site not responding. Last check: 2007-10-09)
A site on an enzyme which upon binding of a modulator, causes the protein to undergo a conformational change that may alter the catalytic or binding properties of the enzyme.
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All intellectual property rights in and to the game are owned in the U.S.A and Canada by Hasbro Inc., and throughout the rest of the world by J.W. Spear & Sons Limited of Maidenhead, Berkshire, England, a subsidiary of Mattel Inc. Mattel and Spear are not affiliated with Hasbro.
www.websters-online-dictionary.org /definition/english/Al/Allosteric%20Site.html   (173 words)

  
 Re: Allosteric site and active site   (Site not responding. Last check: 2007-10-09)
Basically, the allosteric site and the active site work in conjunction with each other.
The use of each site depends on how much or how little the pathway needs to produce.
This type of inhibitor binds to the allosteric site to change the shape of the enzyme and block the pathway.
www.ar.cc.mn.us /ccdiscussion/biology/_disc5/000001ca.htm   (129 words)

  
 The Cys292-->Ala substitution in protein R1 of class I ribonucleotide reductase from Escherichia coli has a global ...   (Site not responding. Last check: 2007-10-09)
The Cys292-->Ala substitution in protein R1 of class I ribonucleotide reductase from Escherichia coli has a global effect on nucleotide binding at the specificity-determining allosteric site.This residue was earlier shown to be specifically photoaffinity labelled with the allosteric nucleotide dTTP.
Ribonucleotide reductase from aerobically grown Escherichia coli is allosterically regulated, both with respect to general activity and substrate specificity.
Protein R1, the homodimeric enzyme component which harbours binding sites for allosteric effectors (nucleoside triphosphates) as well as substrates (ribonucleoside diphosphates), has been engineered at Cys292 close to the dimer interaction area.
www.pdg.cnb.uam.es /UniPub/iHOP/gp/800434.html   (202 words)

  
 Cooperativity in Transcription Factor Binding to the Coactivator CREB-binding Protein (CBP). THE MIXED LINEAGE LEUKEMIA ...
that the MLL-binding site on KIX is distinct from the surface
MLL binds to a distinct site on KIX that is remote from the hydrophobic
Shown is the MLL19 peptide sequence encompassing the core region of the minimal activation domain from human (h) MLL (24), in alignment with analogous regions from mouse (m) and the pufferfish Takifugu rubripes (p) MLL and the human paralogue MLL2.
www.jbc.org /cgi/content/full/277/45/43168   (5805 words)

  
 BIOL 230 Lecture Guide - Allosteric Enzymes   (Site not responding. Last check: 2007-10-09)
Allosteric Enzymes in the Absence of an Inhibitor
An allosteric enzyme has both an active site for its substrate and an allosteric site for an inhibitor of the enzyme.
If the inhibitor is present, it will bind to the enzyme's allosteric site.
www.cat.cc.md.us /courses/bio141/lecguide/unit2/viruses/allonormal.html   (86 words)

  
 Sequence and characteristics of the Bifidobacterium longum gene encoding L-lactate dehydrogenase and the primary ...   (Site not responding. Last check: 2007-10-09)
Sequence and characteristics of the Bifidobacterium longum gene encoding L-lactate dehydrogenase and the primary structure of the enzyme: a new feature of the allosteric site.
Sequence and characteristics of the Bifidobacterium longum gene encoding L-lactate dehydrogenase and the primary structure of the enzyme: a new feature of the allosteric site.Therefore, the B. longum ldh gene might form a monocistronic unit.
Although the B. longum LDH was regulated by FBP, the charge properties of aa residues in the putative FBP-binding site of the LDH were closer to those of the vertebrate LDHs than to those of bacterial LDHs.
www.pdg.cnb.uam.es /UniPub/iHOP/gp/4962.html   (259 words)

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