Literature DB >> 17889251

OMP decarboxylase--An enigma persists.

Brian P Callahan1, Brian G Miller.   

Abstract

In 1995, Radzicka and Wolfenden reported that the rate enhancement produced by orotidine 5'-phosphate decarboxylase (ODCase) approaches 10(17), making this enzyme the most effective pure protein catalyst known in Nature [A. Radzicka, R. Wolfenden, Science 267 (1995) 90-93]. Over the last 12 years, there have been many hypotheses put forward to explain that impressive effect. In this perspective, we provide a summary of the reaction pathways under consideration for ODCase, highlight the supporting and refuting data, and suggest experiments designed to further test each of the candidate pathways.

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Year:  2007        PMID: 17889251     DOI: 10.1016/j.bioorg.2007.07.004

Source DB:  PubMed          Journal:  Bioorg Chem        ISSN: 0045-2068            Impact factor:   5.275


  12 in total

1.  Product deuterium isotope effects for orotidine 5'-monophosphate decarboxylase: effect of changing substrate and enzyme structure on the partitioning of the vinyl carbanion reaction intermediate.

Authors:  Krisztina Toth; Tina L Amyes; Bryant M Wood; Kui Chan; John A Gerlt; John P Richard
Journal:  J Am Chem Soc       Date:  2010-05-26       Impact factor: 15.419

2.  The identification and characteristics of salinity-related microRNAs in gills of Portunus trituberculatus.

Authors:  Jianjian Lv; Ping Liu; Baoquan Gao; Jian Li
Journal:  Cell Stress Chaperones       Date:  2015-09-15       Impact factor: 3.667

3.  The use of reaction timecourses to determine the level of minor contaminants in enzyme preparations.

Authors:  Lawrence M Goldman; Tina L Amyes
Journal:  Anal Biochem       Date:  2014-01-03       Impact factor: 3.365

4.  Dissecting the total transition state stabilization provided by amino acid side chains at orotidine 5'-monophosphate decarboxylase: a two-part substrate approach.

Authors:  Shonoi A Barnett; Tina L Amyes; Bryant M Wood; John A Gerlt; John P Richard
Journal:  Biochemistry       Date:  2008-07-04       Impact factor: 3.162

5.  Proton transfer from C-6 of uridine 5'-monophosphate catalyzed by orotidine 5'-monophosphate decarboxylase: formation and stability of a vinyl carbanion intermediate and the effect of a 5-fluoro substituent.

Authors:  Wing-Yin Tsang; B McKay Wood; Freeman M Wong; Weiming Wu; John A Gerlt; Tina L Amyes; John P Richard
Journal:  J Am Chem Soc       Date:  2012-08-21       Impact factor: 15.419

6.  OMP decarboxylase: phosphodianion binding energy is used to stabilize a vinyl carbanion intermediate.

Authors:  Bogdana Goryanova; Tina L Amyes; John A Gerlt; John P Richard
Journal:  J Am Chem Soc       Date:  2011-04-12       Impact factor: 15.419

7.  Determination of the amino acid sequence requirements for catalysis by the highly proficient orotidine monophosphate decarboxylase.

Authors:  Ji Yuan; Ana Maria Cardenas; Hiram F Gilbert; Timothy Palzkill
Journal:  Protein Sci       Date:  2011-09-22       Impact factor: 6.725

8.  An examination of the relationship between active site loop size and thermodynamic activation parameters for orotidine 5'-monophosphate decarboxylase from mesophilic and thermophilic organisms.

Authors:  Krisztina Toth; Tina L Amyes; B McKay Wood; Kui K Chan; John A Gerlt; John P Richard
Journal:  Biochemistry       Date:  2009-08-25       Impact factor: 3.162

9.  Catalysis in Enzymatic Decarboxylations: Comparison of Selected Cofactor-dependent and Cofactor-independent Examples.

Authors:  Frank Jordan; Hetalben Patel
Journal:  ACS Catal       Date:  2013-07-05       Impact factor: 13.084

10.  Enzyme architecture: deconstruction of the enzyme-activating phosphodianion interactions of orotidine 5'-monophosphate decarboxylase.

Authors:  Lawrence M Goldman; Tina L Amyes; Bogdana Goryanova; John A Gerlt; John P Richard
Journal:  J Am Chem Soc       Date:  2014-07-02       Impact factor: 15.419

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