About: Deregulation of acetohydroxy-acid synthase: loss of allosteric inhibition conferred by mutations in the catalytic subunit     Goto   Sponge   NotDistinct   Permalink

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  • The ilvB genes coding for acetohydroxy acid synthase (AHAS) catalytic subunit from the Streptomyces cinnamonensis parental strain and four mutants deregulated in valine biosynthesis were sequenced. Two changes in the sequence of IlvB conferring the AHAS insensitivity to valine were found in mutant strains: E139A and dQ217. Homology modeling revealed that the substitution E139A is located in a loop at the homodimer subunit-subunit interface near the TPP binding site while dQ217 is situated in a distant helix. Sequencing of ilvBNC upstream region revealed a sequence containing a putative attenuator. However, no mutation within this region was found in mutants with constitutively increased AHAS activity levels suggesting a different mechanism of deregulation
  • The ilvB genes coding for acetohydroxy acid synthase (AHAS) catalytic subunit from the Streptomyces cinnamonensis parental strain and four mutants deregulated in valine biosynthesis were sequenced. Two changes in the sequence of IlvB conferring the AHAS insensitivity to valine were found in mutant strains: E139A and dQ217. Homology modeling revealed that the substitution E139A is located in a loop at the homodimer subunit-subunit interface near the TPP binding site while dQ217 is situated in a distant helix. Sequencing of ilvBNC upstream region revealed a sequence containing a putative attenuator. However, no mutation within this region was found in mutants with constitutively increased AHAS activity levels suggesting a different mechanism of deregulation (en)
  • Byly osekvenovány geny ilvB kódující katalytickou podjednotku syntázy kyseliny hydroxyoctové (AHAS) ze Streptomyces cinamonensis a čtyř dalších mutant, blokovaných v biosyntéze valinu. V mutantních kmenech byly nalezeny dvě změny v genu IlvB, mající za následek ztrátu citlivosti AHAS k valinu: E139A a dQ217. Homologní modelování ukázalo, že substituce E139A je lokalizována ve smyčce v prostoru mezi podjednotkami homodimeru v blízkosti TPP vazebného místa. dQ217 je naproti tomu situována na vzdáleném helixu. Sekvenování oblasti proti směru přepisu ilvBNC odhalilo sekvenci obsahující pravděpodobný atenuátor, ovšem u mutantních kmenů s konstitutivně zvýšenou aktivitou AHAS nebyla v této oblasti žádná mutace nalezena. Na základě tohoto poznatku předpokládáme jiný mechanizmus deregulace (cs)
Title
  • Deregulation of acetohydroxy-acid synthase: loss of allosteric inhibition conferred by mutations in the catalytic subunit
  • Deregulace syntázy kyseliny hydroxyoctové: ztráta alosterické inhibice zapřičiněná mutací v katalytické podjednotce (cs)
  • Deregulation of acetohydroxy-acid synthase: loss of allosteric inhibition conferred by mutations in the catalytic subunit (en)
skos:prefLabel
  • Deregulation of acetohydroxy-acid synthase: loss of allosteric inhibition conferred by mutations in the catalytic subunit
  • Deregulace syntázy kyseliny hydroxyoctové: ztráta alosterické inhibice zapřičiněná mutací v katalytické podjednotce (cs)
  • Deregulation of acetohydroxy-acid synthase: loss of allosteric inhibition conferred by mutations in the catalytic subunit (en)
skos:notation
  • RIV/61388971:_____/08:00320746!RIV09-AV0-61388971
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(GA204/01/1001), P(GA204/05/0616), Z(AV0Z50200510)
http://linked.open...iv/cisloPeriodika
  • 6
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
  • 362590
http://linked.open...ai/riv/idVysledku
  • RIV/61388971:_____/08:00320746
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • acetohydroxy acid; ilvb genes; sequencing (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • CZ - Česká republika
http://linked.open...ontrolniKodProRIV
  • [CB1938D8C455]
http://linked.open...i/riv/nazevZdroje
  • Folia Microbiologica
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 53
http://linked.open...iv/tvurceVysledku
  • Kyselková, Martina
  • Kopecký, Jan
  • Pospíšil, Stanislav
  • Felsberg, Jürgen
  • Janata, Jiří
  • Spížek, Jaroslav
  • Šigutová, Lucie
http://linked.open...ain/vavai/riv/wos
  • 000262754600001
http://linked.open...n/vavai/riv/zamer
issn
  • 0015-5632
number of pages
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