1rqe

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[[Image:1rqe.png|left|200px]]
 
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{{STRUCTURE_1rqe| PDB=1rqe | SCENE= }}
{{STRUCTURE_1rqe| PDB=1rqe | SCENE= }}
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===Propionibacterium shermanii transcarboxylase 5S subunit bound to oxaloacetate===
===Propionibacterium shermanii transcarboxylase 5S subunit bound to oxaloacetate===
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{{ABSTRACT_PUBMED_15329673}}
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==Function==
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[[http://www.uniprot.org/uniprot/5S_PROFR 5S_PROFR]] The 5S subunit specifically catalyzes the transfer of the carboxyl group from biotin of the 1.3S subunit to pyruvate to form oxaloacetate and 1.3S biotin.
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{{ABSTRACT_PUBMED_15329673}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:015329673</ref><ref group="xtra">PMID:014993680</ref><references group="xtra"/>
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<ref group="xtra">PMID:015329673</ref><references group="xtra"/><references/>
[[Category: Methylmalonyl-CoA carboxytransferase]]
[[Category: Methylmalonyl-CoA carboxytransferase]]
[[Category: Propionibacterium freudenreichii subsp. shermanii]]
[[Category: Propionibacterium freudenreichii subsp. shermanii]]

Revision as of 10:58, 16 April 2014

Template:STRUCTURE 1rqe

Contents

Propionibacterium shermanii transcarboxylase 5S subunit bound to oxaloacetate

Template:ABSTRACT PUBMED 15329673

Function

[5S_PROFR] The 5S subunit specifically catalyzes the transfer of the carboxyl group from biotin of the 1.3S subunit to pyruvate to form oxaloacetate and 1.3S biotin.

About this Structure

1rqe is a 1 chain structure with sequence from Propionibacterium freudenreichii subsp. shermanii. Full crystallographic information is available from OCA.

Reference

  • Hall PR, Zheng R, Antony L, Pusztai-Carey M, Carey PR, Yee VC. Transcarboxylase 5S structures: assembly and catalytic mechanism of a multienzyme complex subunit. EMBO J. 2004 Sep 15;23(18):3621-31. Epub 2004 Aug 26. PMID:15329673 doi:http://dx.doi.org/10.1038/sj.emboj.7600373

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