Abstract:
:Glucarate dehydratase (GlucD) from Pseudomonas putida catalyzes the dehydration of both (D)-glucarate and (L)-idarate to 3-deoxy-(L)-threo-2-hexulosarate as well as their epimerization. (D)-[6-13C]Glucarate and (L)-[6-13C]idarate have been synthesized for use in continuous assay of the reactions catalyzed by GlucD by both 13C and 1H NMR spectroscopies, thereby allowing the simultaneous measure of both the dehydration and epimerization reactions. Substrate and solvent isotope effects for the dehydration reactions have been quantitated. The mechanism of the GlucD-catalyzed reaction is discussed in the context of that previously established for the homologous mandelate racemase from P. putida, also a member of the enolase superfamily whose members catalyze reactions initiated by abstraction of a proton alpha to a carboxylate group.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Palmer DR,Hubbard BK,Gerlt JAdoi
10.1021/bi981122vsubject
Has Abstractpub_date
1998-10-13 00:00:00pages
14350-7issue
41eissn
0006-2960issn
1520-4995pii
bi981122vjournal_volume
37pub_type
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