PMID:8253713 - Revision history

imported>Wikientrybot: change PMID template to TableEdit version

2013-09-15T04:53:38Z

change PMID template to TableEdit version

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	'''~~No author listed~~''' (1993) In vitro heme O synthesis by the cyoE gene product from Escherichia coli. ''J. Biol. Chem.'' '''268''':26041-4		'''Saiki, K, Mogi, T, Ogura, K and Anraku, Y''' (1993) In vitro heme O synthesis by the cyoE gene product from Escherichia coli. ''J. Biol. Chem.'' '''268''':26041-4
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imported>Wikientrybot: replace GO_table_reference with annotationlinks

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imported>Wikientrybot: change PMID template to TableEdit version

2013-09-01T19:44:52Z

change PMID template to TableEdit version

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	~~<span style~~ = '~~font-size: large~~'> '~~''Saiki, K, Mogi, T, Ogura, K and Anraku, Y~~''' (1993) In vitro heme O synthesis by the cyoE gene product from Escherichia coli.''J. Biol. Chem.'' '''268''':26041-4</~~span>~~		\|-
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			'''No author listed''' (1993) In vitro heme O synthesis by the cyoE gene product from Escherichia coli. ''J. Biol. Chem.'' '''268''':26041-4
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			!align=left \|Abstract
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			The cytochrome bo complex is a heme-copper terminal quinol oxidase in the aerobic respiratory chain of Escherichia coli and contains low spin heme B, high spin heme O and CuB as the redox metal centers in subunit I. Based on site-directed mutagenesis studies on the cyoE gene in the cytochrome bo operon, we have postulated that the cyoE gene encodes a protoheme IX farnesyltransferase (heme O synthase) (Saiki, K., Mogi, T., and Anraku, Y. (1992) Biochem. Biophys. Res. Commun. 189, 1491-1497). The present study demonstrates that the CyoE protein is localized in the cytoplasmic membrane and that the CyoE-overproduced membranes efficiently catalyze a conversion of exogenous ferrous protoheme IX and farnesyl diphosphate to heme O in the presence of divalent cations such as Mg2+ or Ca2+. Thus, the cyoABCDE operon in E. coli encodes not only subunits of the cytochrome bo complex but also heme O synthase that is specifically required for functional expression of the bo-type quinol oxidase. Heme O seems to be an intermediate in heme A biosynthesis.
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			[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8253713 PubMed]

	~~{\|{{Prettytable}} align = 'center' width= '70%'~~
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	\|~~{{TableHeadingColor}}~~ \|~~'''Abstract'''~~ \|~~\| The cytochrome bo complex is a heme-copper terminal quinol oxidase in the aerobic respiratory chain of~~ Escherichia coli and contains low spin heme B, high spin heme O and CuB as the redox metal centers in subunit I. Based on site-directed mutagenesis studies on the cyoE gene in the cytochrome bo operon, we have postulated that the cyoE gene encodes a protoheme IX farnesyltransferase (heme O synthase) (Saiki, K., Mogi, T., and Anraku, Y. (1992) Biochem. Biophys. Res. Commun. 189, 1491-1497). The present study demonstrates that the CyoE protein is localized in the cytoplasmic membrane and that the CyoE-overproduced membranes efficiently catalyze a conversion of exogenous ferrous protoheme IX and farnesyl diphosphate to heme O in the presence of divalent cations such as Mg2+ or Ca2+. Thus, the cyoABCDE operon in E. coli ~~encodes not only subunits of the cytochrome bo complex but also heme O synthase that is specifically required for functional expression of the bo-type quinol oxidase.~~ Heme ~~O seems to be an intermediate in heme A~~ biosynthesis.		!align=left \|Keywords
	~~</noinclude>~~		\|\|
	\|-		Alkyl and Aryl Transferases; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Cytochrome b Group; Cytochromes/genetics; Cytochromes/metabolism; Escherichia coli/enzymology; Escherichia coli/metabolism; Escherichia coli Proteins; Ferrochelatase/genetics; Ferrochelatase/metabolism; Heme/biosynthesis
	\|{{~~TableHeadingColor~~}} ~~nowrap \|'''Links''' \|\| [http~~:~~//www~~.~~ncbi~~.~~nlm.nih.gov/entrez/query.fcgi?cmd~~=~~Retrieve~~&db=~~pubmed~~&~~dopt~~=~~Abstract~~&~~list_uids~~=~~8253713 PubMed~~]
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	==Significance {{HelpIcon\|Help:Literature}} ==		==Significance {{HelpIcon\|Help:Literature}} ==
	{{LitSignificance}}		{{LitSignificance}}

127.0.0.1: /Volumes/r3/t3/ul/working/touchTables/touch_all_tables.php

2010-06-17T21:12:33Z

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	!\|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status		!\|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

127.0.0.1: Update TableEdit tables.

2010-01-09T04:57:41Z

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imported>Wikientrybot: Fix links due to TableEditLinks.php changes.

2009-02-20T06:38:32Z

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127.0.0.1: Edited by wikibot

2008-04-30T11:54:56Z

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127.0.0.1: Edited by wikibot

2008-04-25T22:03:40Z

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	==Significance {{HelpIcon\|Help:Literature}} ==		==Significance {{HelpIcon\|Help:Literature}} ==
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	==EcoliWiki Links {{HelpIcon\|Help:Literature}} ==		==EcoliWiki Links {{HelpIcon\|Help:Literature}} ==

66.249.70.122: New PMID: Page!

2007-07-24T00:39:01Z

New PMID: Page!

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<span style = 'font-size: large'> '''Saiki, K, Mogi, T, Ogura, K and Anraku, Y''' (1993) In vitro heme O synthesis by the cyoE gene product from Escherichia coli.''J. Biol. Chem.'' '''268''':26041-4</span>

{|{{Prettytable}} align = 'center' width= '70%'
|-
|{{TableHeadingColor}} |'''Abstract''' || The cytochrome bo complex is a heme-copper terminal quinol oxidase in the aerobic respiratory chain of Escherichia coli and contains low spin heme B, high spin heme O and CuB as the redox metal centers in subunit I. Based on site-directed mutagenesis studies on the cyoE gene in the cytochrome bo operon, we have postulated that the cyoE gene encodes a protoheme IX farnesyltransferase (heme O synthase) (Saiki, K., Mogi, T., and Anraku, Y. (1992) Biochem. Biophys. Res. Commun. 189, 1491-1497). The present study demonstrates that the CyoE protein is localized in the cytoplasmic membrane and that the CyoE-overproduced membranes efficiently catalyze a conversion of exogenous ferrous protoheme IX and farnesyl diphosphate to heme O in the presence of divalent cations such as Mg2+ or Ca2+. Thus, the cyoABCDE operon in E. coli encodes not only subunits of the cytochrome bo complex but also heme O synthase that is specifically required for functional expression of the bo-type quinol oxidase. Heme O seems to be an intermediate in heme A biosynthesis.
</noinclude>
|-
|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8253713 PubMed]
|}
</protect>
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}

== Useful Materials and Methods {{HelpIcon|Help:Literature}}==
{{LitMaterials}}

==Annotations {{HelpIcon|Help:Literature}}==
<protect>
[{{SERVER}}/colipedia/index.php/Special:TableEdit?id=63ce1649aab8b3180235b0af7618f667.0.I46a54a25eabc5&page=0&pagename={{FULLPAGENAMEE}}&type=0 Add GO annotations]
</protect>

==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
{{LitLinks}}

==References==
{{RefHelp}}
<references/>