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Glutamine Synthetase: Metals and Filament Coordination
Glutamine Synthetase: Metals and Filament Coordination
Glutamine Synthetase: Metals and Filament Coordination

상세정보

자료유형  
 학위논문 서양
최종처리일시  
20250211152803
ISBN  
9798384094760
DDC  
574
저자명  
Muniz, Richard Sammy.
서명/저자  
Glutamine Synthetase: Metals and Filament Coordination
발행사항  
[Sl] : University of Washington, 2024
발행사항  
Ann Arbor : ProQuest Dissertations & Theses, 2024
형태사항  
73 p
주기사항  
Source: Dissertations Abstracts International, Volume: 86-03, Section: B.
주기사항  
Advisor: Kollman, Jusitn.
학위논문주기  
Thesis (Ph.D.)--University of Washington, 2024.
초록/해제  
요약Glutamine has a central role in cellular metabolism because it is a key donor of carbon and nitrogen atoms to other key metabolic precursors. Nitrogen fixation and mobilization is controlled through the inter-conversion of glutamate and glutamine by glutamine synthetase (GS). GS converts glutamate and ammonium into glutamine in an ATP-dependent reaction. GS assembles into filaments whose formation is conserved among E. coli, yeast, and plants. The higher-order structural organization observed among GS's and the importance of the glutamine pool within metabolism suggest these filaments may serve as a layer of regulation as seen with other filament-forming enzymes. Here we characterized in vitro assembly of E. coli and human glutamine synthetase. We show that the filament formation of E. coli GS is pH and divalent cation-dependent. Additionally, we show metals disrupt active site integrity through secondary structure changes. Finally, we formally show human GS can form filaments, define the residues involved in assembly, and provide structural evidence that these filaments bind and turnover substrates.
일반주제명  
Biochemistry
일반주제명  
Cellular biology
일반주제명  
Molecular biology
키워드  
Glutamine
키워드  
Ammonium
키워드  
Glutamine synthetase
키워드  
Metals
키워드  
Filament formation
기타저자  
University of Washington Molecular and Cellular Biology
기본자료저록  
Dissertations Abstracts International. 86-03B.
전자적 위치 및 접속  
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MARC

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■006m          o    d                
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■020    ▼a9798384094760
■035    ▼a(MiAaPQ)AAI31556853
■040    ▼aMiAaPQ▼cMiAaPQ
■0820  ▼a574
■1001  ▼aMuniz,  Richard  Sammy.
■24510▼aGlutamine  Synthetase:  Metals  and  Filament  Coordination
■260    ▼a[Sl]▼bUniversity  of  Washington▼c2024
■260  1▼aAnn  Arbor▼bProQuest  Dissertations  &  Theses▼c2024
■300    ▼a73  p
■500    ▼aSource:  Dissertations  Abstracts  International,  Volume:  86-03,  Section:  B.
■500    ▼aAdvisor:  Kollman,  Jusitn.
■5021  ▼aThesis  (Ph.D.)--University  of  Washington,  2024.
■520    ▼aGlutamine  has  a  central  role  in  cellular  metabolism  because  it  is  a  key  donor  of  carbon  and  nitrogen  atoms  to  other  key  metabolic  precursors.  Nitrogen  fixation  and  mobilization  is  controlled  through  the  inter-conversion  of  glutamate  and  glutamine  by  glutamine  synthetase  (GS).  GS  converts  glutamate  and  ammonium  into  glutamine  in  an  ATP-dependent  reaction.  GS  assembles  into  filaments  whose  formation  is  conserved  among  E.  coli,  yeast,  and  plants.  The  higher-order  structural  organization  observed  among  GS's  and  the  importance  of  the  glutamine  pool  within  metabolism  suggest  these  filaments  may  serve  as  a  layer  of  regulation  as  seen  with  other  filament-forming  enzymes.  Here  we  characterized  in  vitro  assembly  of  E.  coli  and  human  glutamine  synthetase.  We  show  that  the  filament  formation  of  E.  coli  GS  is  pH  and  divalent  cation-dependent.  Additionally,  we  show  metals  disrupt  active  site  integrity  through  secondary  structure  changes.  Finally,  we  formally  show  human  GS  can  form  filaments,  define  the  residues  involved  in  assembly,  and  provide  structural  evidence  that  these  filaments  bind  and  turnover  substrates.
■590    ▼aSchool  code:  0250.
■650  4▼aBiochemistry
■650  4▼aCellular  biology
■650  4▼aMolecular  biology
■653    ▼aGlutamine
■653    ▼aAmmonium  
■653    ▼aGlutamine  synthetase
■653    ▼aMetals
■653    ▼aFilament  formation  
■690    ▼a0487
■690    ▼a0379
■690    ▼a0307
■71020▼aUniversity  of  Washington▼bMolecular  and  Cellular  Biology.
■7730  ▼tDissertations  Abstracts  International▼g86-03B.
■790    ▼a0250
■791    ▼aPh.D.
■792    ▼a2024
■793    ▼aEnglish
■85640▼uhttp://www.riss.kr/pdu/ddodLink.do?id=T17163867▼nKERIS▼z이  자료의  원문은  한국교육학술정보원에서  제공합니다.

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