About: Structural and Functional Energetic Linkages in Allosteric Regulation of Muscle Pyruvate Kinase     Goto   Sponge   Distinct   Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

AttributesValues
rdf:type
rdfs:seeAlso
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. (en)
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 (en)
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 (en)
skos:notation
  • RIV/00216208:11320/11:10105045!RIV12-MSM-11320___
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • Z(MSM0021620835)
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 232723
http://linked.open...ai/riv/idVysledku
  • RIV/00216208:11320/11:10105045
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • Kinase; Pyruvate; Muscle; Regulation; Allosteric; Linkages; Energetic; Functional; Structural (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...ontrolniKodProRIV
  • [3E370275803E]
http://linked.open...i/riv/mistoVydani
  • Oxford
http://linked.open...vEdiceCisloSvazku
  • Biothermodynamics, Part C, 488
http://linked.open...i/riv/nazevZdroje
  • Methods in Enzymology
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...v/pocetStranKnihy
http://linked.open...cetTvurcuVysledku
http://linked.open...UplatneniVysledku
http://linked.open...iv/tvurceVysledku
  • Heřman, Petr
  • Lee, J. C.
http://linked.open...n/vavai/riv/zamer
number of pages
http://bibframe.org/vocab/doi
  • 10.1016/B978-0-12-381268-1.00008-2
http://purl.org/ne...btex#hasPublisher
  • Academic Press
https://schema.org/isbn
  • 978-0-12-381268-1
http://localhost/t...ganizacniJednotka
  • 11320
Faceted Search & Find service v1.16.118 as of Jun 21 2024


Alternative Linked Data Documents: ODE     Content Formats:   [cxml] [csv]     RDF   [text] [turtle] [ld+json] [rdf+json] [rdf+xml]     ODATA   [atom+xml] [odata+json]     Microdata   [microdata+json] [html]    About   
This material is Open Knowledge   W3C Semantic Web Technology [RDF Data] Valid XHTML + RDFa
OpenLink Virtuoso version 07.20.3240 as of Jun 21 2024, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (126 GB total memory, 112 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software