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Title Stereochemistry and function of oxaloacetate keto-enol tautomerase
Creator/Author Creighton, D.J. ; Johnson, J.D. ; Lambert, M.R.
Publication Date1986 May 01
OSTI IdentifierOSTI ID: 5418088
Report Number(s)CONF-8606151-
Other Number(s)CODEN: FEPRA
Resource TypeConference
Specific TypeJournal Article
Resource RelationFed. Proc., Fed. Am. Soc. Exp. Biol. ; Vol/Issue: 45:6; 76. annual meeting of the Federation of American Society for Experimental Biology; 8 Jun 1986; Washington, DC, USA
Research OrgUniv. of Maryland Baltimore County, Catonsville
Subject550201 -- Biochemistry-- Tracer Techniques; ISOMERASES-- BIOCHEMICAL REACTION KINETICS;ISOMERASES-- STEREOCHEMISTRY; ENZYME ACTIVITY;NADH2;TRACER TECHNIQUES;TRITIUM COMPOUNDS
Related SubjectCOENZYMES;ENZYMES;ISOTOPE APPLICATIONS;KINETICS;LABELLED COMPOUNDS;NUCLEOTIDES;ORGANIC COMPOUNDS;REACTION KINETICS
Description/Abstract Oxaloacetate keto-enol tautomerase, partially purified from porcine kidney, catalyzes the conversions of enol- to keto-oxaloacetate by a mechanism in which solvent protons end up equally distributed between the two prochiral positions at C3 of keto-oxaloacetate.^This conclusion is based upon the observation that when enzyme catalyzed ketonization is conducted in /sup 3/H/sub 2/O in the presence of excess malate dehydrogenase and NADH, only 50% of the /sup 3/H in the isolated (2S)-(3-/sup 3/H)malate is labilized to solvent upon treatment with fumarase.^Either the tautomerase operates on the basis of a highly unusual stereomechanistic principle or tautomerase activity is not an evolved property of the enzyme protein.^As a result of an attempt to clarify the physiological importance of oxaloacetate tautomerase activity, keto-oxaloacetate was demonstrated to be directly transported across the inner membrane of rat liver mitochrondria, on the basis of the results of kinetic and isotope-trapping experiments.
Country of PublicationUnited States
LanguageEnglish
FormatPages: 1502
System Entry Date2001 May 13

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