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3oxo

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m (Protected "3oxo" [edit=sysop:move=sysop])
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[[Image:3oxo.png|left|200px]]
 
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{{STRUCTURE_3oxo| PDB=3oxo | SCENE= }}
{{STRUCTURE_3oxo| PDB=3oxo | SCENE= }}
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===Succinyl-CoA:3-ketoacid CoA transferase from pig heart covalently bound to CoA===
===Succinyl-CoA:3-ketoacid CoA transferase from pig heart covalently bound to CoA===
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{{ABSTRACT_PUBMED_20977214}}
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==Function==
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[[http://www.uniprot.org/uniprot/SCOT1_PIG SCOT1_PIG]] Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate.
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(as it appears on PubMed at http://www.pubmed.gov), where 20977214 is the PubMed ID number.
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{{ABSTRACT_PUBMED_20977214}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:20977214</ref><references group="xtra"/>
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<ref group="xtra">PMID:020977214</ref><references group="xtra"/><references/>
[[Category: 3-oxoacid CoA-transferase]]
[[Category: 3-oxoacid CoA-transferase]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Fraser, M E.]]
[[Category: Fraser, M E.]]
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[[Category: Alpha/beta protein]]
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[[Category: Transferase]]

Revision as of 08:29, 2 May 2013

Template:STRUCTURE 3oxo

Contents

Succinyl-CoA:3-ketoacid CoA transferase from pig heart covalently bound to CoA

Template:ABSTRACT PUBMED 20977214

Function

[SCOT1_PIG] Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate.

About this Structure

3oxo is a 8 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA.

Reference

  • Fraser ME, Hayakawa K, Brown WD. Catalytic Role of the Conformational Change in Succinyl-CoA:3-Oxoacid CoA Transferase on Binding CoA. Biochemistry. 2010 Oct 26. PMID:20977214 doi:10.1021/bi100659s

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