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Statements

Subject Item
n2:RIV%2F00216208%3A11320%2F11%3A10105045%21RIV12-MSM-11320___
rdf:type
n7:Vysledek skos:Concept
rdfs:seeAlso
http://www.sciencedirect.com/science/article/pii/B9780123812681000082
dcterms:description
RMPK is a homotetramer. Each subunit consists of 530 amino acids and multiple domains. The active site resides between the A and B domains. Besides the basic TIM-barrel motif, RMPK also exhibits looped-out regions in the α/β barrel of each monomer forming the B- and C-domains. The two isozymes of PK, namely, the kidney and muscle isozymes, exhibit very different allosteric behaviors under the same experimental condition. The only amino acid sequence differences between the mammalian kidney and muscle PK isozymes are located in the C-domain and are involved in intersubunit interactions. Thus, embedded in these two isozymes of PK are the rules involved in engineering the popular TIM (α/β)8 motif to modulate its allosteric properties. The PK system exhibits a lot of the properties that will allow mining of the ground rules governing the correlative linkages between sequence-fold-function. In this chapter, we review the approaches to acquire the fundamental functional and structural energetics that establish the linkages among this intricate network of linked multiequilibria. Results from these diverse approaches are integrated to establish a working model to represent the complex network of multiple linked reactions which ultimately leads to the observation of allosteric regulation of PK. RMPK is a homotetramer. Each subunit consists of 530 amino acids and multiple domains. The active site resides between the A and B domains. Besides the basic TIM-barrel motif, RMPK also exhibits looped-out regions in the α/β barrel of each monomer forming the B- and C-domains. The two isozymes of PK, namely, the kidney and muscle isozymes, exhibit very different allosteric behaviors under the same experimental condition. The only amino acid sequence differences between the mammalian kidney and muscle PK isozymes are located in the C-domain and are involved in intersubunit interactions. Thus, embedded in these two isozymes of PK are the rules involved in engineering the popular TIM (α/β)8 motif to modulate its allosteric properties. The PK system exhibits a lot of the properties that will allow mining of the ground rules governing the correlative linkages between sequence-fold-function. In this chapter, we review the approaches to acquire the fundamental functional and structural energetics that establish the linkages among this intricate network of linked multiequilibria. Results from these diverse approaches are integrated to establish a working model to represent the complex network of multiple linked reactions which ultimately leads to the observation of allosteric regulation of PK.
dcterms:title
Structural and Functional Energetic Linkages in Allosteric Regulation of Muscle Pyruvate Kinase Structural and Functional Energetic Linkages in Allosteric Regulation of Muscle Pyruvate Kinase
skos:prefLabel
Structural and Functional Energetic Linkages in Allosteric Regulation of Muscle Pyruvate Kinase Structural and Functional Energetic Linkages in Allosteric Regulation of Muscle Pyruvate Kinase
skos:notation
RIV/00216208:11320/11:10105045!RIV12-MSM-11320___
n7:predkladatel
n20:orjk%3A11320
n4:aktivita
n13:Z
n4:aktivity
Z(MSM0021620835)
n4:dodaniDat
n12:2012
n4:domaciTvurceVysledku
n17:7948395
n4:druhVysledku
n22:C
n4:duvernostUdaju
n11:S
n4:entitaPredkladatele
n5:predkladatel
n4:idSjednocenehoVysledku
232723
n4:idVysledku
RIV/00216208:11320/11:10105045
n4:jazykVysledku
n18:eng
n4:klicovaSlova
Kinase; Pyruvate; Muscle; Regulation; Allosteric; Linkages; Energetic; Functional; Structural
n4:klicoveSlovo
n10:Structural n10:Energetic n10:Regulation n10:Linkages n10:Functional n10:Muscle n10:Kinase n10:Allosteric n10:Pyruvate
n4:kontrolniKodProRIV
[3E370275803E]
n4:mistoVydani
Oxford
n4:nazevEdiceCisloSvazku
Biothermodynamics, Part C, 488
n4:nazevZdroje
Methods in Enzymology
n4:obor
n21:CE
n4:pocetDomacichTvurcuVysledku
1
n4:pocetStranKnihy
401
n4:pocetTvurcuVysledku
2
n4:rokUplatneniVysledku
n12:2011
n4:tvurceVysledku
Heřman, Petr Lee, J. C.
n4:zamer
n14:MSM0021620835
s:numberOfPages
33
n9:doi
10.1016/B978-0-12-381268-1.00008-2
n23:hasPublisher
Academic Press
n6:isbn
978-0-12-381268-1
n16:organizacniJednotka
11320