About: Functional assignments for the carboxyl-terminal domains of the ferrochelatase from Synechocystis PCC 6803: The CAB domain plays a regulatory role, and region II is essential for catalysis

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About: Functional assignments for the carboxyl-terminal domains of the ferrochelatase from Synechocystis PCC 6803: The CAB domain plays a regulatory role, and region II is essential for catalysis Goto Sponge NotDistinct Permalink

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	Ferrochelatase (FeCH) catalyses the insertion of Fe2+ into protoporphyrin forming protoheme. In photosynthetic organisms FeCH and Mg-chelatase lie at a biosynthetic branchpoint where partitioning down the heme and chlorophyll pathways occurs. Unlike their mammalian, yeast and other bacterial counterparts cyanobacterial and algal FeCHs as well as FeCH2 isoform from plants possess a C-terminal CAB domain with a putative chlorophyll-binding motif. We found that the CAB domain in the cyanobacterium Synechocystis 6803 is not required for catalytic activity but is essential for dimerization of FeCH and its absence causes aberrant accumulation of chlorophyll-protein complexes under high light accompanied by high levels of the chlorophyll precursor chlorophyllide Ferrochelatase (FeCH) catalyses the insertion of Fe2+ into protoporphyrin forming protoheme. In photosynthetic organisms FeCH and Mg-chelatase lie at a biosynthetic branchpoint where partitioning down the heme and chlorophyll pathways occurs. Unlike their mammalian, yeast and other bacterial counterparts cyanobacterial and algal FeCHs as well as FeCH2 isoform from plants possess a C-terminal CAB domain with a putative chlorophyll-binding motif. We found that the CAB domain in the cyanobacterium Synechocystis 6803 is not required for catalytic activity but is essential for dimerization of FeCH and its absence causes aberrant accumulation of chlorophyll-protein complexes under high light accompanied by high levels of the chlorophyll precursor chlorophyllide (en)
Title	Functional assignments for the carboxyl-terminal domains of the ferrochelatase from Synechocystis PCC 6803: The CAB domain plays a regulatory role, and region II is essential for catalysis Functional assignments for the carboxyl-terminal domains of the ferrochelatase from Synechocystis PCC 6803: The CAB domain plays a regulatory role, and region II is essential for catalysis (en)
skos:prefLabel	Functional assignments for the carboxyl-terminal domains of the ferrochelatase from Synechocystis PCC 6803: The CAB domain plays a regulatory role, and region II is essential for catalysis Functional assignments for the carboxyl-terminal domains of the ferrochelatase from Synechocystis PCC 6803: The CAB domain plays a regulatory role, and region II is essential for catalysis (en)
skos:notation	RIV/61388971:_____/11:00362757!RIV12-AV0-61388971
http://linked.open...avai/predkladatel	Mikrobiologický ústav AV ČR, v.v.i.
http://linked.open...avai/riv/aktivita	P Z
http://linked.open...avai/riv/aktivity	P(GAP501/10/1000), Z(AV0Z50200510), Z(MSM6007665808)
http://linked.open...iv/cisloPeriodika	4
http://linked.open...vai/riv/dodaniDat	2012
http://linked.open...aciTvurceVysledku	Tichý, Martin Sobotka, Roman
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Mikrobiologický ústav AV ČR, v. v. i.
http://linked.open...dnocenehoVysledku	200519
http://linked.open...ai/riv/idVysledku	RIV/61388971:_____/11:00362757
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	TRANSFER-RNA REDUCTASE; DELTA-AMINOLEVULINIC-ACID; PHOTOSYSTEM-II (en)
http://linked.open.../riv/klicoveSlovo	DELTA-AMINOLEVULINIC-ACID PHOTOSYSTEM-II TRANSFER-RNA REDUCTASE
http://linked.open...odStatuVydavatele	US - Spojené státy americké
http://linked.open...ontrolniKodProRIV	[E7618A123526]
http://linked.open...i/riv/nazevZdroje	Plant Physiology
http://linked.open...in/vavai/riv/obor	EE
http://linked.open...ichTvurcuVysledku	2 (xsd:int)
http://linked.open...cetTvurcuVysledku	4 (xsd:int)
http://linked.open...vavai/riv/projekt	Identification and localization of protein complexes involved in the regulation of chlorophyll biosynthesis
http://linked.open...UplatneniVysledku	2011
http://linked.open...v/svazekPeriodika	155
http://linked.open...iv/tvurceVysledku	Hunter, C. N. Sobotka, Roman Tichý, Martin Wilde, A.
http://linked.open...ain/vavai/riv/wos	000289095500025
http://linked.open...n/vavai/riv/zamer	Microorganisms in Research and Biotechnology Fyzikální biologie -nové přístupy v biologickém výzkumu
issn	0032-0889
number of pages	13 (xsd:int)
http://bibframe.org/vocab/doi	10.1104/pp.110.167528
is http://linked.open...avai/riv/vysledek of	Functional assignments for the carboxyl-terminal domains of the ferrochelatase from Synechocystis PCC 6803: The CAB domain plays a regulatory role, and region II is essential for catalysis Functional assignments for the carboxyl-terminal domains of the ferrochelatase from Synechocystis PCC 6803: The CAB domain plays a regulatory role, and region II is essential for catalysis

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