4kp2

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m (Protected "4kp2" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_4kp2| PDB=4kp2 | SCENE= }}
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===Crystal structure of homoaconitase large subunit from methanococcus jannaschii (MJ1003)===
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{{ABSTRACT_PUBMED_24699638}}
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The entry 4kp2 is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/HACA_METJA HACA_METJA]] Hydro-lyase with broad substrate specificity for cis-unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4-tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4-tricarboxylate), and its hydration to homoisocitrate ((1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate). Is also able to hydrate the analogous longer chain substrates cis-homo(2)-aconitate, cis-homo(3)-aconitate, and even the non-physiological cis-homo(4)-aconitate with similar efficiency. These reactions are part of the biosynthesis pathway of coenzyme B. Can also catalyze the hydration of maleate to (R)-malate, and that of cis-aconitate. Can not catalyze the hydration of citraconate and the dehydration of (S)-homocitrate, citramalate, 2-isopropylmalate, 3-isopropylmalate, citrate or threo-DL-isocitrate.<ref>PMID:17449626</ref> <ref>PMID:18765671</ref> <ref>PMID:20170198</ref>
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Authors: Hwang, K.Y., Lee, E.H.
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==About this Structure==
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[[4kp2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KP2 OCA].
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Description: Crystal structure of homoaconitase large subunit from methanococcus jannaschii (MJ1003)
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==Reference==
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<ref group="xtra">PMID:024699638</ref><references group="xtra"/><references/>
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[[Category: Hwang, K Y.]]
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[[Category: Lee, E H.]]
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[[Category: Aconitase family]]
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[[Category: Alpha-beta-alpha 3-layer sandwich]]
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[[Category: Iron-sulfur cluster binding]]
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[[Category: Isomerase]]
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[[Category: Lyase]]

Revision as of 07:40, 23 April 2014

Template:STRUCTURE 4kp2

Contents

Crystal structure of homoaconitase large subunit from methanococcus jannaschii (MJ1003)

Template:ABSTRACT PUBMED 24699638

Function

[HACA_METJA] Hydro-lyase with broad substrate specificity for cis-unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4-tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4-tricarboxylate), and its hydration to homoisocitrate ((1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate). Is also able to hydrate the analogous longer chain substrates cis-homo(2)-aconitate, cis-homo(3)-aconitate, and even the non-physiological cis-homo(4)-aconitate with similar efficiency. These reactions are part of the biosynthesis pathway of coenzyme B. Can also catalyze the hydration of maleate to (R)-malate, and that of cis-aconitate. Can not catalyze the hydration of citraconate and the dehydration of (S)-homocitrate, citramalate, 2-isopropylmalate, 3-isopropylmalate, citrate or threo-DL-isocitrate.[1] [2] [3]

About this Structure

4kp2 is a 2 chain structure. Full crystallographic information is available from OCA.

Reference

  • Lee EH, Lee K, Hwang KY. Structural characterization and comparison of the large subunits of IPM isomerase and homoaconitase from Methanococcus jannaschii. Acta Crystallogr D Biol Crystallogr. 2014 Apr 1;70(Pt 4):922-31. doi:, 10.1107/S1399004713033762. Epub 2014 Mar 19. PMID:24699638 doi:http://dx.doi.org/10.1107/S1399004713033762
  1. ↑ Drevland RM, Waheed A, Graham DE. Enzymology and evolution of the pyruvate pathway to 2-oxobutyrate in Methanocaldococcus jannaschii. J Bacteriol. 2007 Jun;189(12):4391-400. Epub 2007 Apr 20. PMID:17449626 doi:http://dx.doi.org/10.1128/JB.00166-07
  2. ↑ Drevland RM, Jia Y, Palmer DR, Graham DE. Methanogen homoaconitase catalyzes both hydrolyase reactions in coenzyme B biosynthesis. J Biol Chem. 2008 Oct 24;283(43):28888-96. Epub 2008 Sep 2. PMID:18765671 doi:http://dx.doi.org/M802159200
  3. ↑ Jeyakanthan J, Drevland RM, Gayathri DR, Velmurugan D, Shinkai A, Kuramitsu S, Yokoyama S, Graham DE. Substrate specificity determinants of the methanogen homoaconitase enzyme: structure and function of the small subunit. Biochemistry. 2010 Mar 30;49(12):2687-96. PMID:20170198 doi:10.1021/bi901766z

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