| Attributes | Values |
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| rdf:type
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| Description
| - Heme and chlorophyll (Chl) share a common biosynthetic pathway up to the branch point where magnesium chelatase and ferrochelatase (FeCH) insert either magnesium for Chl biosynthesis or ferrous iron for heme biosynthesis. A distinctive feature of FeCHs in cyanobacteria is their C-terminal extension, which forms a putative transmembrane segment containing a Chl-binding motif. We analyzed the Delta H324 strain of Synechocystis sp. strain PCC 6803, which contains a truncated FeCH enzyme lacking this C-terminal domain. Truncated FeCH was localized to the membrane fraction, suggesting that the C-terminal domain is not necessary for membrane association of the enzyme. Measurements of enzyme activity and complementation experiments revealed that the Delta H324 mutation dramatically reduced activity of the FeCH, which resulted in highly upregulated 5-aminolevulinic acid synthesis in the Delta H324 mutant, implying a direct role for heme in the regulation of flux through the pathway. Moreover, the Delta H324 m
- Heme and chlorophyll (Chl) share a common biosynthetic pathway up to the branch point where magnesium chelatase and ferrochelatase (FeCH) insert either magnesium for Chl biosynthesis or ferrous iron for heme biosynthesis. A distinctive feature of FeCHs in cyanobacteria is their C-terminal extension, which forms a putative transmembrane segment containing a Chl-binding motif. We analyzed the Delta H324 strain of Synechocystis sp. strain PCC 6803, which contains a truncated FeCH enzyme lacking this C-terminal domain. Truncated FeCH was localized to the membrane fraction, suggesting that the C-terminal domain is not necessary for membrane association of the enzyme. Measurements of enzyme activity and complementation experiments revealed that the Delta H324 mutation dramatically reduced activity of the FeCH, which resulted in highly upregulated 5-aminolevulinic acid synthesis in the Delta H324 mutant, implying a direct role for heme in the regulation of flux through the pathway. Moreover, the Delta H324 m (en)
- Analyzovali jsme kmen sinice Synechocystis sp. PCC 6803, obsahující zkrácenou formu enzymu ferochelatázy bez C-koncové domény. Zkráceny enzym byl lokalizován v membránové frakci, což ukazuje, že doména není nezbytná pro asociaci enzymu s membránou. Z měření aktivit a z komplementace vyplývalo, že mutace DH324 dramaticky redukuje aktivitu ferochelatázy. Mimoto, mutant DH324 akumuloval velká množství protoporfyrinu and prekurzorů chlorofylu. Analýza rekombinantní úplné a zkrácené ferochelatatázy prokázala, že C-koncová doména je nezbytná pro aktivitu enzymu and pro jeho oligomerizaci. (cs)
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| Title
| - The C-Terminal extension of ferrochelatase is critical for enzyme aktivity and for functioning of the tetrapyrrole pathway in Synechocystis strain PCC 6803
- The C-Terminal extension of ferrochelatase is critical for enzyme aktivity and for functioning of the tetrapyrrole pathway in Synechocystis strain PCC 6803 (en)
- C-terminální extenze enzymu ferochelatázy je nezbytná pro aktivitu enzymu a pro fungování biosyntetické dráhy tetrapyrolů u Synechocystis PCC6830 (cs)
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| skos:prefLabel
| - The C-Terminal extension of ferrochelatase is critical for enzyme aktivity and for functioning of the tetrapyrrole pathway in Synechocystis strain PCC 6803
- The C-Terminal extension of ferrochelatase is critical for enzyme aktivity and for functioning of the tetrapyrrole pathway in Synechocystis strain PCC 6803 (en)
- C-terminální extenze enzymu ferochelatázy je nezbytná pro aktivitu enzymu a pro fungování biosyntetické dráhy tetrapyrolů u Synechocystis PCC6830 (cs)
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| skos:notation
| - RIV/60076658:12640/08:00009368!RIV09-MSM-12640___
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| http://linked.open...avai/riv/aktivita
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| http://linked.open...avai/riv/aktivity
| - Z(AV0Z50200510), Z(MSM6007665808)
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| http://linked.open...iv/cisloPeriodika
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| http://linked.open...vai/riv/dodaniDat
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| http://linked.open...aciTvurceVysledku
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| http://linked.open.../riv/druhVysledku
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| http://linked.open...iv/duvernostUdaju
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| http://linked.open...titaPredkladatele
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| http://linked.open...dnocenehoVysledku
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| http://linked.open...ai/riv/idVysledku
| - RIV/60076658:12640/08:00009368
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| http://linked.open...riv/jazykVysledku
| |
| http://linked.open.../riv/klicovaSlova
| - transfer-rna reductase; sp PCC 6803; photosystem-II; biosynthetic-pathway; heme-biosynthesis; Escherichia-coli; higher-plants; Chlamydomonas-reinhardtii; Saccharomyces-cerevisiae; magnesium chelatase (en)
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| http://linked.open.../riv/klicoveSlovo
| |
| http://linked.open...odStatuVydavatele
| - US - Spojené státy americké
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| http://linked.open...ontrolniKodProRIV
| |
| http://linked.open...i/riv/nazevZdroje
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| http://linked.open...in/vavai/riv/obor
| |
| http://linked.open...ichTvurcuVysledku
| |
| http://linked.open...cetTvurcuVysledku
| |
| http://linked.open...UplatneniVysledku
| |
| http://linked.open...v/svazekPeriodika
| |
| http://linked.open...iv/tvurceVysledku
| - Sobotka, Roman
- Tichý, Martin
- Hunter, Neil
- McLean, Samantha
- Zuberova, Monika
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| http://linked.open...ain/vavai/riv/wos
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| http://linked.open...n/vavai/riv/zamer
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| issn
| |
| number of pages
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| http://localhost/t...ganizacniJednotka
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