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'''MUCONATE LACTONIZING ENZYME FROM PSEUDOMONAS PUTIDA''' | '''MUCONATE LACTONIZING ENZYME FROM PSEUDOMONAS PUTIDA''' | ||
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[[Category: Schlichting, I.]] | [[Category: Schlichting, I.]] | ||
[[Category: Taylor, K.]] | [[Category: Taylor, K.]] | ||
[[Category: | [[Category: Isomerase]] | ||
[[Category: | [[Category: Muconate cycloisomerase aromatic hydrocarbons catabolism]] | ||
[[Category: | [[Category: Muconate lactonizing enzyme]] | ||
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Revision as of 11:38, 2 May 2008
MUCONATE LACTONIZING ENZYME FROM PSEUDOMONAS PUTIDA
OverviewOverview
Muconate lactonizing enzyme (MLE), a component of the beta-ketoadipate pathway of Pseudomonas putida, is a member of a family of related enzymes (the "enolase superfamily") that catalyze the abstraction of the alpha-proton of a carboxylic acid in the context of different overall reactions. New untwinned crystal forms of MLE were obtained, one of which diffracts to better than 2.0-A resolution. The packing of the octameric enzyme in this crystal form is unusual, because the asymmetric unit contains three subunits. The structure of MLE presented here contains no bound metal ion, but is very similar to a recently determined Mn2+-bound structure. Thus, absence of the metal ion does not perturb the structure of the active site. The structures of enolase, mandelate racemase, and MLE were superimposed. A comparison of metal ligands suggests that enolase may retain some characteristics of the ancestor of this enzyme family. Comparison of other residues involved in catalysis indicates two unusual patterns of conservation: (i) that the position of catalytic atoms remains constant, although the residues that contain them are located at different points in the protein fold; and (ii) that the positions of catalytic residues in the protein scaffold are conserved, whereas their identities and roles in catalysis vary.
About this StructureAbout this Structure
1BKH is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.
ReferenceReference
Evolution of an enzyme active site: the structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolase., Hasson MS, Schlichting I, Moulai J, Taylor K, Barrett W, Kenyon GL, Babbitt PC, Gerlt JA, Petsko GA, Ringe D, Proc Natl Acad Sci U S A. 1998 Sep 1;95(18):10396-401. PMID:9724714 Page seeded by OCA on Fri May 2 11:37:59 2008