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Morpheein

Model of protein allosteric regulation

Morpheein
Summary

Model of protein allosteric regulation

Proteins that function as morpheeins are illustrated using a dice analogy where one die can morph into two different shapes, cubic and tetrahedral. The illustrated assemblies apply a rule that the die face with one spot must contact the die face with four spots. To satisfy the rule for each die in an assembly, the cubic dice can only form a tetramer and the tetrahedral dice can only assemble to a pentamer. This is analogous to two different conformations (morpheein forms) of a protein subunit each dictating assembly to a different oligomer. All dice in one assembly must be of the same shape before assembly. Thus, for example, the tetramer must come apart, and its component dice must change shape to a pyramid before they can participate in assembly into a pentamer.

Morpheeins are proteins that can form two or more different homo-oligomers (morpheein forms), but must come apart and change shape to convert between forms. The alternate shape may reassemble to a different oligomer. The shape of the subunit dictates which oligomer is formed. Each oligomer has a finite number of subunits (stoichiometry). Morpheeins can interconvert between forms under physiological conditions and can exist as an equilibrium of different oligomers. These oligomers are physiologically relevant and are not misfolded protein; this distinguishes morpheeins from prions and amyloid. The different oligomers have distinct functionality. Interconversion of morpheein forms can be a structural basis for allosteric regulation, an idea noted many years ago, A mutation that shifts the normal equilibrium of morpheein forms can serve as the basis for a conformational disease. Features of morpheeins can be exploited for drug discovery. The dice image (Fig 1) represents a morpheein equilibrium containing two different monomeric shapes that dictate assembly to a tetramer or a pentamer. The one protein that is established to function as a morpheein is porphobilinogen synthase, though there are suggestions throughout the literature that other proteins may function as morpheeins (for more information see "Table of Putative Morpheeins" below).

Implications for drug discovery

Implications for allosteric regulation

The morpheein model of allosteric regulation has similarities to and differences from other models. The concerted model (the Monod, Wyman and Changeux (MWC) model) of allosteric regulation requires all subunits to be in the same conformation or state within an oligomer like the morpheein model. However, neither this model nor the sequential model (Koshland, Nemethy, and Filmer model) takes into account that the protein may dissociate to interconvert between oligomers. Nonetheless, shortly after these theories were described, two groups of workers{{cite journal | doi-access = free

Implications for teaching about protein structure-function relationships

It is generally taught that a given amino acid sequence will have only one physiologically relevant (native) quaternary structure; morpheeins challenge this concept. The morpheein model does not require gross changes in the basic protein fold. The conformational differences that accompany conversion between oligomers may be similar to the protein motions necessary for function of some proteins. The morpheein model highlights the importance of conformational flexibility for protein functionality and offers a potential explanation for proteins showing non-Michaelis-Menten kinetics, hysteresis, and/or protein concentration dependent specific activity.

Implications for understanding the structural basis for disease

The term "conformational disease" generally encompasses mutations that result in misfolded proteins that aggregate, such as Alzheimer's and Creutzfeldt–Jakob diseases. In light of the discovery of morpheeins, however, this definition could be expanded to include mutations that shift an equilibrium of alternate oligomeric forms of a protein. An example of such a conformational disease is ALAD porphyria, which results from a mutation of porphobilinogen synthase that causes a shift in its morpheein equilibrium.

Table of proteins whose published behavior is consistent with that of a morpheein

ProteinExample speciesEC numberCAS numberAlternate oligomersEvidence
Acetyl-CoA carboxylase-1Gallus domesticusdoi=10.1042/BST20060223title=Regulation of acetyl-CoA carboxylaseyear=2006last1=Boonefirst1=A.N.last2=Brownseyfirst2=R.W.last3=Elliottfirst3=J.E.last4=Kulpafirst4=J.E.last5=Leefirst5=W.M.journal=Biochemical Society Transactionsvolume=34issue=2pages=223–7pmid=16545081}}doi=10.1016/j.molcel.2004.11.034title=A Mechanism for the Potent Inhibition of Eukaryotic Acetyl-Coenzyme a Carboxylase by Soraphen A, a Macrocyclic Polyketide Natural Productyear=2004last1=Shenfirst1=Yanglast2=Volrathfirst2=Sandra L.last3=Weatherlyfirst3=Stephanie C.last4=Elichfirst4=Tedd D.last5=Tongfirst5=Liangjournal=Molecular Cellvolume=16issue=6pages=881–91pmid=15610732doi-access=free }} Multiple/protein moonlighting functions
α-AcetylgalactosaminidaseBos taurusdoi=10.1021/bi00782a021title=Association-dissociation and abnormal kinetics of bovine .alpha.-acetylgalactosaminidaseyear=1971last1=Weissmannfirst1=Bernardlast2=Wangfirst2=Ching-Tejournal=Biochemistryvolume=10issue=6pages=1067–72pmid=5550813}}doi=10.1021/bi00833a038title=Mammalian α-acetylgalactosaminidase. Occurrence, partial purification, and action on linkages in submaxillary mucinsyear=1969last1=Weissmannfirst1=Bernardlast2=Hinrichsenfirst2=Dorotea F.journal=Biochemistryvolume=8issue=5pages=2034–43pmid=5785223}} Different assemblies have different activities, Conformationally distinct oligomeric forms.
Adenylosuccinate lyaseBacillus subtilisdoi=10.1021/bi701400ctitle=Evaluation of Types of Interactions in Subunit Association in Bacillus subtilis Adenylosuccinate Lyaseyear=2008last1=De Zoysa Ariyanandafirst1=Lushantilast2=Colmanfirst2=Roberta F.journal=Biochemistryvolume=47issue=9pages=2923–34pmid=18237141}}first1=Jennifer Brosiuslast1=Palencharfirst2=Roberta F.last2=Colmanyear=2003title=Characterization of a Mutant Bacillus subtilis Adenylosuccinate Lyase Equivalent to a Mutant Enzyme Found in Human Adenylosuccinate Lyase Deficiency: Asparagine 276 Plays an Important Structural Rolejournal=Biochemistryvolume=42issue=7pages=1831–41doi=10.1021/bi020640+pmid=12590570}} Oligomer-dependent kinetic parameters, Protein concentration dependent molecular weight
Aristolochene synthasePenicillium roquefortidoi=10.1016/0003-9861(89)90204-Xtitle=Purification and characterization of the sesquiterpene cyclase aristolochene synthase from Penicillium roquefortiyear=1989last1=Hohnfirst1=Thomas M.last2=Plattnerfirst2=Ronald D.journal=Archives of Biochemistry and Biophysicsvolume=272pages=137–43pmid=2544140issue=1}}doi=10.1074/jbc.M000433200title=Crystal Structure Determination of Aristolochene Synthase from the Blue Cheese Mold, Penicillium roquefortiyear=2000last1=Caruthersfirst1=J. M.journal=Journal of Biological Chemistryvolume=275issue=33pages=25533–9pmid=10825154last2=Kangfirst2=Ilast3=Rynkiewiczfirst3=MJlast4=Canefirst4=DElast5=Christiansonauthor5-link=David W. Christiansonfirst5=DWdoi-access=free }}
L-AsparaginaseLeptosphaeria michotiidoi=10.1111/j.1399-3054.1985.tb01215.xtitle=L-Asparaginase activity in Leptosphaeria michotii. Isolation and properties of two forms of the enzymeyear=1985last1=Jerebzoff-Quintinfirst1=Simonnelast2=Jerebzofffirst2=Stephanjournal=Physiologia Plantarumvolume=64pages=74–80}}doi=10.1016/j.jmb.2007.03.061pmc=1991333title=Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia coli l-Asparaginase Iyear=2007last1=Yunfirst1=Mi-Kyunglast2=Noursefirst2=Amandalast3=Whitefirst3=Stephen W.last4=Rockfirst4=Charles O.last5=Heathfirst5=Richard J.journal=Journal of Molecular Biologyvolume=369issue=3pages=794–811pmid=17451745}}
AspartokinaseEscherichia coli&doi=10.1073/pnas.77.6.3379pmid=6774337title=Sequential Folding of a Bifunctional Allosteric Proteinyear=1980last1=Garelfirst1=J.-R.journal=Proceedings of the National Academy of Sciencesvolume=77issue=6bibcode=1980PNAS...77.3379Gjstor=8892pages=3379–3383pmc=349619doi-access=free }}pmid=163250year=1975last1=Ogilviefirst1=JWlast2=Vickersfirst2=LPlast3=Clarkfirst3=RBlast4=Jonesfirst4=MMtitle=Aspartokinase I-homoserine dehydrogenase I of Escherichia coli K12 (lambda). Activation by monovalent cations and an analysis of the effect of the adenosine triphosphate-magnesium ion complex on this activation processvolume=250issue=4pages=1242–50journal=The Journal of Biological Chemistrydoi=10.1016/S0021-9258(19)41805-Xdoi-access=free }} Conformationally distinct oligomeric forms
ATPase of the ABCA1 transporterHomo sapiensdoi=10.1074/jbc.M601072200title=Transition from Dimers to Higher Oligomeric Forms Occurs during the ATPase Cycle of the ABCA1 Transporteryear=2006last1=Trompierfirst1=D.journal=Journal of Biological Chemistryvolume=281issue=29pages=20283–90pmid=16709568last2=Alibertfirst2=Mlast3=Davanturefirst3=Slast4=Hamonfirst4=Ylast5=Pierresfirst5=Mlast6=Chiminifirst6=Gdoi-access=free }}Substrate binding/turnover impacts multimerization
Biotin—(acetyl-CoA-carboxylase) ligase holoenzyme synthetaseEscherichia colidoi=10.1021/bi991241qtitle=Dimerization of theEscherichiacoliBiotin Repressor: Corepressor Function in Protein Assemblyyear=1999last1=Eisensteinfirst1=Edwardlast2=Beckettfirst2=Dorothyjournal=Biochemistryvolume=38issue=40pages=13077–84pmid=10529178}}doi=10.1021/bi9715019title=Coupling of Site-Specific DNA Binding to Protein Dimerization in Assembly of the Biotin Repressor−Biotin Operator Complexyear=1998last1=Streakerfirst1=Emily D.last2=Beckettfirst2=Dorothyjournal=Biochemistryvolume=37issue=9pages=3210–9pmid=9485476}}
Chorismate mutaseEscherichia colidimer, trimer, hexamerdoi=10.1110/ps.051431605pmc=2279322title=Simultaneous optimization of enzyme activity and quaternary structure by directed evolutionyear=2005last1=Vamvacafirst1=Katherinalast2=Butzfirst2=Marenlast3=Walterfirst3=Kai U.last4=Taylorfirst4=Sean V.last5=Hilvertfirst5=Donaldjournal=Protein Sciencevolume=14issue=8pages=2103–14pmid=15987889}}
Citrate synthaseEscherichia colidoi=10.1021/bi00673a007title=Quaternary structure of citrate synthase from Escherichia coli K 12year=1975last1=Tongfirst1=E. K.last2=Duckworthfirst2=Harry W.journal=Biochemistryvolume=14issue=2pages=235–41pmid=1091285}}Substrate binding/turnover impacts multimerization, Characterized equilibrium of oligomers, Protein concentration dependent specific activity, pH-dependent oligomeric equilibrium
Cyanovirin-NNostoc ellipsosporumdoi=10.1038/828title=Solution structure of cyanovirin-N, a potent HIV-inactivating proteinyear=1998last1=Bewleyfirst1=Carole A.last2=Gustafsonfirst2=Kirk R.last3=Boydfirst3=Michael R.last4=Covellfirst4=David G.last5=Baxfirst5=Adlast6=Clorefirst6=G. Mariuslast7=Gronenbornfirst7=Angela M.journal=Nature Structural Biologyvolume=5issue=7pages=571–8pmid=9665171s2cid=11367037 }}pmid=15638789year=2005last1=Barrientosfirst1=LGlast2=Gronenbornfirst2=AMtitle=The highly specific carbohydrate-binding protein cyanovirin-N: Structure, anti-HIV/Ebola activity and possibilities for therapyvolume=5issue=1pages=21–31journal=Mini Reviews in Medicinal Chemistrydoi=10.2174/1389557053402783}} Conformationally distinct oligomeric forms
3-oxoacid CoA-transferaseSus scrofa domesticadoi=10.1021/bi0003184title=Pig Heart CoA Transferase Exists as Two Oligomeric Forms Separated by a Large Kinetic Barrieryear=2000last1=Rochetfirst1=Jean-Christophelast2=Browniefirst2=Edward R.last3=Oikawafirst3=Kimlast4=Hicksfirst4=Leslie D.last5=Fraserfirst5=Marie E.last6=Jamesfirst6=Michael N. G.last7=Kayfirst7=Cyril M.last8=Bridgerfirst8=William A.last9=Wolodkofirst9=William T.display-authors=8journal=Biochemistryvolume=39issue=37pages=11291–302pmid=10985774}}Chromatographically separable oligomers, Substrate might preferentially stabilize one form
Cystathionine β-synthaseHomo sapiensdoi=10.1021/bi060737mtitle=Solvent-Accessible Cysteines in Human Cystathionine β-Synthase: Crucial Role of Cysteine 431 inS-Adenosyl-l-methionine Bindingyear=2006last1=Frankfirst1=Ninalast2=Keryfirst2=Vladimirlast3=MacLeanfirst3=Kenneth N.last4=Krausfirst4=Jan P.journal=Biochemistryvolume=45issue=36pages=11021–9pmid=16953589}}doi=10.1021/bi602617fpmc=3204387title=A Pathogenic Linked Mutation in the Catalytic Core of Human Cystathionine β-Synthase Disrupts Allosteric Regulation and Allows Kinetic Characterization of a Full-Length Dimeryear=2007last1=Senfirst1=Suvajitlast2=Banerjeefirst2=Rumajournal=Biochemistryvolume=46issue=13pages=4110–6pmid=17352495}} Mutations shift the equilibrium of oligomers, Different assemblies have different activities, disease-causing mutations at sites distant from active site
D-amino acid oxidasepmid=4380380year=1966last1=Antoninifirst1=Elast2=Brunorifirst2=Mlast3=Bruzzesifirst3=Rlast4=Chianconefirst4=Elast5=Masseyfirst5=Vtitle=Association-dissociation phenomena of D-amino acid oxidasevolume=241issue=10pages=2358–66journal=The Journal of Biological Chemistrydoi=10.1016/S0021-9258(18)96629-9doi-access=free }}Oligomer-dependent kinetic parameters
Dihydrolipoamide dehydrogenaseSus scrofa domesticadoi=10.1073/pnas.0610618104pmc=1851069title=Cryptic proteolytic activity of dihydrolipoamide dehydrogenaseyear=2007last1=Babadyfirst1=N. E.last2=Pangfirst2=Y.-P.last3=Elpelegfirst3=O.last4=Isayafirst4=G.journal=Proceedings of the National Academy of Sciencesvolume=104issue=15pages=6158–63bibcode = 2007PNAS..104.6158Bpmid=17404228doi-access=free }}doi=10.1111/j.1432-1033.1973.tb02679.xtitle=Conformational Studies on Lipoamide Dehydrogenase from Pig Heart. 1. Interconversion of Dissociable and Non-Dissociable Formsyear=1973last1=Muiswinkel-Voetbergfirst1=H.last2=Visserfirst2=Jaaplast3=Veegerfirst3=Cornelisjournal=European Journal of Biochemistryvolume=33issue=2pages=265–70pmid=4348439doi-access= }}
Dopamine β-monooxygenaseBos taurusfirst1=Ashimalast1=Saxenafirst2=Prestonlast2=Hensleyfirst3=James C.last3=Osbornefirst4=Patrick J.last4=Flemingyear=1985title=The pH-dependent Subunit Dissociation and Catalytic Activity of Bovine Dopamine β-Hydroxylasejournal=Journal of Biological Chemistrypmid=3972830url=http://www.jbc.org/cgi/pmidlookup?view=long&pmid=3972830volume=260issue=6pages=3386–92doi=10.1016/S0021-9258(19)83633-5doi-access=free }}Effector molecules impact multimerization, Characterized equilibrium of oligomers, Oligomer-dependent kinetic parameters
Geranylgeranyl pyrophosphate synthase / FarnesyltranstransferaseHomo sapiensdoi=10.1074/jbc.274.9.5888title=Human Geranylgeranyl Diphosphate Synthase. CDNA CLONING AND EXPRESSIONyear=1999last1=Kuzuguchifirst1=T.journal=Journal of Biological Chemistryvolume=274issue=9pages=5888–94pmid=10026212last2=Moritafirst2=Ylast3=Sagamifirst3=Ilast4=Sagamifirst4=Hlast5=Ogurafirst5=Kdoi-access= free}}Effector molecules impact multimerization
GDP-mannose 6-dehydrogenasePseudomonas aeruginosadoi=10.1021/bi027328ktitle=Crystal Structure of GDP-Mannose Dehydrogenase: A Key Enzyme of Alginate Biosynthesis inP. Aeruginosayear=2003last1=Snookfirst1=Christopher F.last2=Tiptonfirst2=Peter A.last3=Beamerfirst3=Lesa J.journal=Biochemistryvolume=42issue=16pages=4658–68pmid=12705829}}doi=10.1021/bi025862mtitle=Allosterism and Cooperativity inPseudomonas aeruginosaGDP-Mannose Dehydrogenaseyear=2002last1=Naughtfirst1=Laura E.last2=Gilbertfirst2=Sunnylast3=Imhofffirst3=Rebeccalast4=Snookfirst4=Christopherlast5=Beamerfirst5=Lesalast6=Tiptonfirst6=Peterjournal=Biochemistryvolume=41issue=30pages=9637–45pmid=12135385}} Kinetic hysteresis
Glutamate dehydrogenaseBos taurusdoi=10.1002/9780470122846.ch6chapter=Glutamate Dehydrogenase—ligand Complexes and Their Relationship to the Mechanism of the Reactiontitle=Advances in Enzymology and Related Areas of Molecular Biologyvolume=39year=2006last1=Fisherfirst1=Harvey F.isbn=978-0-470-12284-6pages=369–417pmid=4147773series=Advances in Enzymology - and Related Areas of Molecular Biologychapter-url=https://archive.org/details/advancesinenzymo0039unse/page/369 }}pmid=4402280year=1972last1=Huangfirst1=CYlast2=Friedenfirst2=Ctitle=The mechanism of ligand-induced structural changes in glutamate dehydrogenase. Studies of the rate of depolymerization and isomerization effected by coenzymes and guanine nucleotidesvolume=247issue=11pages=3638–46journal=The Journal of Biological Chemistrydoi=10.1016/S0021-9258(19)45188-0doi-access=free }} Characterized equilibrium of oligomers
Glutamate racemaseMycobacterium tuberculosis, Escherichia coli, Bacillus subtilis, Aquifex pyrophilusdoi=10.1007/s007920050114title=Molecular cloning, expression, and characterization of a thermostable glutamate racemase from a hyperthermophilic bacterium, Aquifex pyrophilusyear=1999last1=Kimfirst1=Sang Suklast2=Choifirst2=I.-G.last3=Kimfirst3=Sung-Houlast4=Yufirst4=Y. G.journal=Extremophilesvolume=3issue=3pages=175–83pmid=10484173s2cid=709039 }}doi=10.1074/jbc.C200253200title=Glutamate Racemase is an Endogenous DNA Gyrase Inhibitoryear=2002last1=Ashiuchifirst1=M.journal=Journal of Biological Chemistryvolume=277issue=42pages=39070–3pmid=12213801last2=Kuwanafirst2=Elast3=Yamamotofirst3=Tlast4=Komatsufirst4=Klast5=Sodafirst5=Klast6=Misonofirst6=Hdoi-access=freehdl=10126/3383hdl-access=free }} Characterized equilibrium of oligomers, Conformationally distinct oligomeric forms
Glyceraldehyde-3-phosphate dehydrogenaseOryctolagus cuniculas, Sus scrofa domesticadoi=10.1016/S0167-4838(99)00119-3title=New insights into an old protein: The functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenaseyear=1999last1=Siroverfirst1=Michael Ajournal=Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymologyvolume=1432issue=2pmid=10407139pages=159–84 }} Characterized equilibrium of oligomers, Different assemblies have different activities
Glycerol kinaseEscherichia colidoi=10.1021/bi00617a011title=Subunit dissociation in the allosteric regulation of glycerol kinase from Escherichia coli. 2. Physical evidenceyear=1978last1=De Rielfirst1=Jon K.last2=Paulusfirst2=Henryjournal=Biochemistryvolume=17issue=24pages=5141–6pmid=215195}}doi=10.1016/S0969-2126(98)00140-3title=Glycerol kinase from Escherichia coli and an Ala65→Thr mutant: The crystal structures reveal conformational changes with implications for allosteric regulationyear=1998last1=Feesefirst1=Michael Dlast2=Faberfirst2=H Ricklast3=Bystromfirst3=Cory Elast4=Pettigrewfirst4=Donald Wlast5=Remingtonfirst5=S Jamesjournal=Structurevolume=6issue=11pages=1407–18pmid=9817843doi-access=free }} Conformationally distinct oligomeric forms, Effector functions by preventing domain motion
HIV-IntegraseHuman immunodeficiency virus-1doi=10.1021/bi000397jtitle=Oligomeric States of the HIV-1 Integrase As Measured by Time-Resolved Fluorescence Anisotropyyear=2000last1=Deprezfirst1=Ericlast2=Taucfirst2=Patricklast3=Lehfirst3=Hervélast4=Mouscadetfirst4=Jean-Françoislast5=Auclairfirst5=Christianlast6=Brochonfirst6=Jean-Claudejournal=Biochemistryvolume=39issue=31pages=9275–84pmid=10924120}}doi=10.1074/jbc.M602198200title=Relationship between the Oligomeric Status of HIV-1 Integrase on DNA and Enzymatic Activityyear=2006last1=Guiotfirst1=E.journal=Journal of Biological Chemistryvolume=281issue=32pages=22707–19pmid=16774912last2=Carayonfirst2=Klast3=Delelisfirst3=Olast4=Simonfirst4=Flast5=Taucfirst5=Plast6=Zubinfirst6=Elast7=Gottikhfirst7=Mlast8=Mouscadetfirst8=JFlast9=Brochonfirst9=JCdisplay-authors=8doi-access=free }} Multiple/protein moonlighting functions, Different assemblies have different activities
HPr-Kinase/phosphataseBacillus subtilis, Lactobacillus casei, Mycoplasma pneumoniae, Staphylococcus xylosus/doi=10.1093/emboj/20.15.3917pmc=149164title=X-ray structure of HPr kinase: A bacterial protein kinase with a P-loop nucleotide-binding domainyear=2001last1=Fieulainefirst1=S.journal=The EMBO Journalvolume=20issue=15pages=3917–27pmid=11483495last2=Morerafirst2=Slast3=Poncetfirst3=Slast4=Monederofirst4=Vlast5=Gueguen-Chaignonfirst5=Vlast6=Galinierfirst6=Alast7=Janinfirst7=Jlast8=Deutscherfirst8=Jlast9=Nesslerfirst9=Sdisplay-authors=8 }}Effector molecules impact multimerization, Multiple/protein moonlighting functions, Different assemblies have different activities, pH-dependent oligomeric equilibrium
Lactate dehydrogenaseBacillus stearothermophilusdoi=10.1016/0167-4838(85)90319-Xtitle=Changes in the state of subunit association of lactate dehydrogenase from Bacillus stearothermophilusyear=1985last1=Clarkefirst1=Anthony R.last2=Waldmanfirst2=Adam D.B.last3=Munrofirst3=Ianlast4=Holbrookfirst4=J.Johnjournal=Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymologyvolume=828issue=3pmid=3986214pages=375–9}}doi=10.1016/0167-4838(87)90234-2title=A single amino acid substitution deregulates a bacterial lactate dehydrogenase and stabilizes its tetrameric structureyear=1987last1=Clarkefirst1=Anthony R.last2=Wigleyfirst2=Dale B.last3=Barstowfirst3=David A.last4=Chiafirst4=William N.last5=Atkinsonfirst5=Tonylast6=Holbrookfirst6=J.Johnjournal=Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymologyvolume=913pmid=3580377pages=72–80issue=1}} Oligomer-dependent kinetic parameters, Conformationally distinct oligomeric forms
Lon proteaseEscherichia coli, Mycobacterium smegmatisdoi=10.1021/bi980945htitle=Functional Role of the N-Terminal Region of the Lon Protease fromMycobacterium smegmatisyear=1998last1=Roudiakfirst1=Stanislav G.last2=Shraderfirst2=Thomas E.journal=Biochemistryvolume=37issue=32pages=11255–63pmid=9698372}}doi=10.1021/bi052377tpmc=2515378title=Single-Turnover Kinetic Experiments Confirm the Existence of High- and Low-Affinity ATPase Sites inEscherichia coliLon Proteaseyear=2006last1=Vineyardfirst1=Dianalast2=Patterson-Wardfirst2=Jessicalast3=Leefirst3=Irenejournal=Biochemistryvolume=45issue=14pages=4602–10pmid=16584195}} Kinetic hysteresis
Mitochondrial NAD(P)+ Malic enzyme / malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)Homo sapiensdoi=10.1016/S0969-2126(02)00788-8title=Molecular Mechanism for the Regulation of Human Mitochondrial NAD(P)+-Dependent Malic Enzyme by ATP and Fumarateyear=2002last1=Yangfirst1=Zhirulast2=Lanksfirst2=Charles W.last3=Tongfirst3=Liangjournal=Structurevolume=10issue=7pages=951–60pmid=12121650doi-access=free }}doi=10.1074/jbc.M109.005082title=Functional Roles of the Tetramer Organization of Malic Enzymeyear=2009last1=Hsiehfirst1=J.-Y.last2=Chenfirst2=S.-H.last3=Hungfirst3=H.-C.journal=Journal of Biological Chemistryvolume=284issue=27pages=18096–105pmid=19416979pmc=2709377doi-access=free }} Kinetic hysteresis,
PeroxiredoxinsSalmonella typhimurium&2 dimers, decamerdoi=10.1016/j.abb.2004.09.006title=Bacterial defenses against oxidants: Mechanistic features of cysteine-based peroxidases and their flavoprotein reductasesyear=2005last1=Poolefirst1=Leslie B.journal=Archives of Biochemistry and Biophysicsvolume=433pages=240–54pmid=15581580issue=1}} Different assemblies have different activities
Phenylalanine hydroxylaseHomo sapiensdoi=10.1046/j.1432-1327.2001.01958.xtitle=A comparison of kinetic and regulatory properties of the tetrameric and dimeric forms of wild-type and Thr427→Pro mutant human phenylalanine hydroxylaseyear=2001last1=Bjørgofirst1=Elisalast2=De Carvalhofirst2=Raquel Margarida Negrãolast3=Flatmarkfirst3=Torgeirauthor3-link=Torgeir Flatmarkjournal=European Journal of Biochemistryvolume=268issue=4pages=997–1005pmid=11179966}}pmid=7887915year=1995last1=Martinezfirst1=Auroralast2=Knappskogfirst2=Per M.last3=Olafsdottirfirst3=Sigridurlast4=Døskelandfirst4=Anne P.last5=Eikenfirst5=Hans Geirlast6=Svebakfirst6=Randi Myrsethlast7=Bozzinifirst7=MeriLisalast8=Apoldfirst8=Jaranlast9=Flatmarkfirst9=Torgeirauthor9-link=Torgeir Flatmarkdisplay-authors=8title=Expression of recombinant human phenylalanine hydroxylase as fusion protein in Escherichia coli circumvents proteolytic degradation by host cell proteases. Isolation and characterization of the wild-type enzymevolume=306issue=2pages=589–97pmc=1136558journal=The Biochemical Journaldoi=10.1042/bj3060589 }} Conformationally distinct oligomeric forms
Phosphoenolpyruvate carboxylaseEscherichia coli, Zea mays{{EnzExplorer4.1.1.31}}pmid=4560418year=1972last1=Wohlfirst1=RClast2=Markusfirst2=Gtitle=Phosphoenolpyruvate carboxylase of Escherichia coli. Purification and some propertiesvolume=247issue=18pages=5785–92journal=The Journal of Biological Chemistrydoi=10.1016/S0021-9258(19)44827-8doi-access=free }}
PhosphofructokinaseBacillus stearothermophilus, Thermus thermophilusdoi=10.1016/S0022-2836(05)80171-8title=Tetramer-dimer conversion of phosphofructokinase from Thermus thermophilus induced by its allosteric effectorsyear=1990last1=Xufirst1=Jinglast2=Oshimafirst2=Tairolast3=Yoshidafirst3=Masasukejournal=Journal of Molecular Biologyvolume=215issue=4pages=597–606pmid=2146397}}Effector molecules impact multimerization, Characterized equilibrium of oligomers
Polyphenol oxidaseAgaricus bisporus, Malus domestica, Lactuca sativa L.pmid=14284774year=1965last1=Jolley Jrfirst1=RLlast2=Masonfirst2=HStitle=The Multiple Forms of Mushroom Tyrosinase. Interconversionvolume=240pages=PC1489–91journal=The Journal of Biological Chemistrydoi=10.1016/S0021-9258(18)97603-9doi-access=free }}pmid=18135760year=1949last1=Mallettefirst1=MFlast2=Dawsonfirst2=CRtitle=On the nature of highly purified mushroom tyrosinase preparationsvolume=23issue=1pages=29–44journal=Archives of Biochemistry}} Substrate binding/turnover impacts multimerization, Different assemblies have different activities, Kinetic hysteresis
Porphobilinogen synthaseDrosophila melanogaster, Danio reriovauthors=Jaffe EK, Lawrence SHtitle = Allostery and the dynamic oligomerization of porphobilinogen synthasejournal = Arch. Biochem. Biophys.volume = 519issue = 2pages = 144–53date=March 2012pmid = 22037356pmc = 3291741doi = 10.1016/j.abb.2011.10.010 }}PBGS is the prototype morpheein.
Pyruvate kinaseHomo sapiensdoi=10.1016/0014-5793(75)90064-2title=Alanine-mediated reversible inactivation of tumour pyruvate kinase caused by a tetramer-dimer transitionyear=1975last1=Schulzfirst1=Ju¨Rgenlast2=Sparmannfirst2=Giselalast3=Hofmannfirst3=Eberhardjournal=FEBS Lettersvolume=50issue=3pages=346–50pmid=1116605s2cid=5665440doi-access=freebibcode=1975FEBSL..50..346S }}Conformationally distinct oligomeric forms
Ribonuclease ABos taurusdoi=10.1110/ps.36602title=Structures of the two 3D domain-swapped RNase a trimersyear=2009last1=Liufirst1=Yanshunlast2=Gottefirst2=Giovannilast3=Libonatifirst3=Massimolast4=Eisenbergfirst4=Davidjournal=Protein Sciencevolume=11issue=2pages=371–80pmid=11790847pmc=2373430}}doi=10.1007/s00018-004-4302-xtitle=Biological actions of the oligomers of ribonuclease Ayear=2004last1=Libonatifirst1=M.journal=Cellular and Molecular Life Sciencesvolume=61issue=19–20pages=2431–6pmid=15526151s2cid=8769502pmc=11924434 }} Different assemblies have different activities, Conformationally distinct oligomeric forms
Ribonucleotide reductaseMus musculusdoi=10.1021/bi020634dtitle=Comprehensive Model for Allosteric Regulation of Mammalian Ribonucleotide Reductase: Refinements and Consequences†year=2003last1=Kashlanfirst1=Ossama B.last2=Coopermanfirst2=Barry S.journal=Biochemistryvolume=42issue=6pages=1696–706pmid=12578384}}Effector molecules impact multimerization
S-adenosyl-L-homocysteine hydrolaseDictyostelium discoideumdoi=10.1016/0003-9861(84)90507-1title=Purification of S-adenosyl-l-homocysteine hydrolase from Dictyostelium discoideum: Reversible inactivation by cAMP and 2′-deoxyadenosineyear=1984last1=Hohmanfirst1=R.J.last2=Guittonfirst2=M.C.last3=Véronfirst3=M.journal=Archives of Biochemistry and Biophysicsvolume=233issue=2pages=785–95pmid=6091559}}Effector molecules impact multimerization
Biodegrative threonine dehydratase / threonine ammonia-lyaseEscherichia colipmid=321452year=1977last1=Saekifirst1=Ylast2=Itofirst2=Slast3=Shizutafirst3=Ylast4=Hayaishifirst4=Olast5=Kagamiyamafirst5=Hlast6=Wadafirst6=Htitle=Subunit structure of biodegradative threonine deaminasevolume=252issue=7pages=2206–8journal=The Journal of Biological Chemistrydoi=10.1016/S0021-9258(17)40542-4doi-access=free }}Effector molecules impact multimerization, Characterized equilibrium of oligomers, Different assemblies have different activities
β-TryptaseHomo sapiensdoi=10.1021/bi960042ttitle=Inactivation of Human Lung Tryptase: Evidence for a Re-Activatable Tetrameric Intermediate and Active Monomersyear=1996last1=Addingtonfirst1=Adele K.last2=Johnsonfirst2=David A.journal=Biochemistryvolume=35issue=42pages=13511–8pmid=8885830}}doi=10.1016/S0167-4838(98)00053-3title=Spontaneous inactivation of human lung tryptase as probed by size-exclusion chromatography and chemical cross-linking: Dissociation of active tetrameric enzyme into inactive monomers is the primary event of the entire processyear=1998last1=Kozikfirst1=Andrzejlast2=Potempafirst2=Janlast3=Travisfirst3=Jamesjournal=Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymologyvolume=1385pmid=9630576pages=139–48issue=1}} Characterized equilibrium of oligomers
Tumor necrosis factor-αHomo sapiensdoi=10.1021/bi00019a012title=Mechanism of suramin-induced deoligomerization of tumor necrosis factor .alphayear=1995last1=Alzanifirst1=R.last2=Cozzifirst2=E.last3=Cortifirst3=A.last4=Temponifirst4=M.last5=Triziofirst5=D.last6=Giglifirst6=M.last7=Rizzofirst7=V.journal=Biochemistryvolume=34issue=19pages=6344–50pmid=7756262}}doi=10.1111/j.1432-1033.1995.0381e.xtitle=The Folding and Assembly Pathway of Tumour Necrosis Factor TNFalpha, a Globular Trimeric Proteinyear=1995last1=Hlodanfirst1=Romanlast2=Painfirst2=Roger H.journal=European Journal of Biochemistryvolume=231issue=2pages=381–7pmid=7635149doi-access=free }}
Uracil phosphoribosyltransferaseEscherichia colidoi=10.1111/j.1432-1033.1996.0637h.xtitle=Different Oligomeric States are Involved in the Allosteric Behavior of Uracil Phosphoribosyltransferase from Escherichia Coliyear=1996last1=Jensenfirst1=Kaj Franklast2=Mygindfirst2=Bentejournal=European Journal of Biochemistryvolume=240issue=3pages=637–45pmid=8856065}}Effector molecules impact multimerization, Substrate binding/turnover impacts multimerization, Different assemblies have different activities

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