4jn6

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==About this Structure==
==About this Structure==
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[[4jn6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JN6 OCA].
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[[4jn6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JN6 OCA].
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==See Also==
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*[[Aldolase|Aldolase]]
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==Reference==
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<ref group="xtra">PMID:023614353</ref><references group="xtra"/><references/>
[[Category: 4-hydroxy-2-oxovalerate aldolase]]
[[Category: 4-hydroxy-2-oxovalerate aldolase]]
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[[Category: Mycobacterium tuberculosis]]
 
[[Category: Carere, J.]]
[[Category: Carere, J.]]
[[Category: Kimber, M S.]]
[[Category: Kimber, M S.]]

Revision as of 12:23, 20 November 2013

Template:STRUCTURE 4jn6

Contents

Crystal Structure of the Aldolase-Dehydrogenase Complex from Mycobacterium tuberculosis HRv37

Template:ABSTRACT PUBMED 23614353

Function

[HOA_MYCTU] Catalyzes the retro-aldol cleavage of 4-hydroxy-2-oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta-cleavage pathway for the degradation of aromatic compounds (By similarity). [ACDH_MYCTU] Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds (By similarity).

About this Structure

4jn6 is a 4 chain structure with sequence from "bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884. Full crystallographic information is available from OCA.

See Also

Reference

  • Carere J, McKenna SE, Kimber MS, Seah SY. Characterization of an aldolase-dehydrogenase complex from the cholesterol degradation pathway of Mycobacterium tuberculosis. Biochemistry. 2013 Apr 24. PMID:23614353 doi:http://dx.doi.org/10.1021/bi400351h

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