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| [[Image:1dub.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1dub| PDB=1dub | SCENE= }} | | {{STRUCTURE_1dub| PDB=1dub | SCENE= }} |
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| '''2-ENOYL-COA HYDRATASE, DATA COLLECTED AT 100 K, PH 6.5'''
| | ===2-ENOYL-COA HYDRATASE, DATA COLLECTED AT 100 K, PH 6.5=== |
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| ==Overview==
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| The crystal structure of rat liver mitochondrial enoyl-coenzyme A (CoA) hydratase complexed with the potent inhibitor acetoacetyl-CoA has been refined at 2.5 angstroms resolution. This enzyme catalyses the reversible addition of water to alpha,beta-unsaturated enoyl-CoA thioesters, with nearly diffusion-controlled reaction rates for the best substrates. Enoyl-CoA hydratase is a hexamer of six identical subunits of 161 kDa molecular mass for the complex. The hexamer is a dimer of trimers. The monomer is folded into a right-handed spiral of four turns, followed by two small domains which are involved in trimerization. Each turn of the spiral consists of two beta-strands and an alpha-helix. The mechanism for the hydratase/dehydratase reaction follows a syn-stereochemistry, a preference that is opposite to the nonenzymatic reaction. The active-site architecture agrees with this stereochemistry. It confirms the importance of Glu164 as the catalytic acid for providing the alpha-proton during the hydratase reaction. It also shows the importance of Glu144 as the catalytic base for the activation of a water molecule in the hydratase reaction. The comparison of an unliganded and a liganded active site within the same crystal form shows a water molecule in the unliganded subunit. This water molecule is bound between the two catalytic glutamates and could serve as the activated water during catalysis. | | The line below this paragraph, {{ABSTRACT_PUBMED_8895557}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 8895557 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_8895557}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Fatty acid metabolism]] | | [[Category: Fatty acid metabolism]] |
| [[Category: Lyase]] | | [[Category: Lyase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:17:01 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:37:39 2008'' |
