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4kp1

From Proteopedia

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'''Unreleased structure'''
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{{STRUCTURE_4kp1| PDB=4kp1 | SCENE= }}
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===Crystal structure of IPM isomerase large subunit from methanococcus jannaschii (MJ0499)===
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{{ABSTRACT_PUBMED_24699638}}
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The entry 4kp1 is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/LEUC_METJA LEUC_METJA]] Enzyme with broad specificity that catalyzes reversible hydroxyacid isomerizations via dehydration/hydration reactions. Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate, a step involved in leucine biosynthesis. Catalyzes the isomerization between 2-methylmalate and 3-methylmalate, via the formation of 2-methylmaleate (citraconate), a step involved in isoleucine biosynthesis. Also displays malease activity, i.e. catalyzes the hydration of maleate to form (R)-malate.<ref>PMID:17449626</ref>
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Authors: Hwang, K.Y., Lee, E.H.
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==About this Structure==
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[[4kp1]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KP1 OCA].
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Description: Crystal structure of IPM isomerase large subunit from methanococcus jannaschii (MJ0499)
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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]]

Revision as of 07:40, 23 April 2014

Template:STRUCTURE 4kp1

Contents

Crystal structure of IPM isomerase large subunit from methanococcus jannaschii (MJ0499)

Template:ABSTRACT PUBMED 24699638

Function

[LEUC_METJA] Enzyme with broad specificity that catalyzes reversible hydroxyacid isomerizations via dehydration/hydration reactions. Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate, a step involved in leucine biosynthesis. Catalyzes the isomerization between 2-methylmalate and 3-methylmalate, via the formation of 2-methylmaleate (citraconate), a step involved in isoleucine biosynthesis. Also displays malease activity, i.e. catalyzes the hydration of maleate to form (R)-malate.[1]

About this Structure

4kp1 is a 1 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

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