HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Pratt, A. G. Articles by Friedkin, M. Search for Related Content PubMed PubMed Citation Articles by Pratt, A. G. Articles by Friedkin, M. Social Bookmarking                      What's this?

The Hydrolysis of Mono-, Di-, and Triglutamate Derivatives of Folic Acid with Bacterial Enzymes

From the ¹ From the Department of Biochemistry, Tufts University School of Medicine, 136 Harrison Avenue, Boston, Massachusetts 02111

A soil organism of the genus Flavobacterium was isolated from a medium containing folic acid as the sole source of carbon and nitrogen (ATCC 25012). This organism resembles but is not identical with a previously described strain, Flavobacterium polyglutamicum. It utilizes the glutamate released from pteroylmonoglutamate by the action of an intracellular enzyme, folate amidase. The relative rates of enzymatic hydrolysis of a variety of analogues of pteroylmonoglutamate were determined in order to characterize the substrate specificity of folate amidase. Gel filtration was used to separate folate amidase from two other bacterial enzymes: one that acts on -glutamylglutamate and another that splits -glutamylglutamate. Enzyme fractions that hydrolyzed -glutamylglutamate also released free glutamate from pteroyl--diglutamate and pteroyl-,-triglutamate.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?