The role of enoyl-CoA hydratase in the metabolism of isoleucine byPseudomonas putida View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1978-04

AUTHORS

Charles M. Roberts, R. S. Conrad, J. R. Sokatch

ABSTRACT

The purpose of the present study was to determine if the enoyl coenzyme A hydratase formed by Pseudomonas putida during growth on isoleucine was a unique enzyme specific for isoleucine metabolism. The highest levels of the hydratase were formed during growth on isoleucine intermediates and the lowest levels during growth on glutamate and glucose. Data from growth experiments revealed that 2-methyl-3-hydroxybutyryl coenzyme A hydratase, an enzyme unique to isoleucine metabolism and enoyl coenzyme A hydratase were coordinately induced, but that 3-hydroxyacyl coenzyme A dehydrogenase was under separate control. The hydratase was purified 180-fold from isoleucine cells, and its physical and catalytic properties reported. The highest activity was with crotonyl coenzyme A,Vmax = 1100 x 10(3) moles/min mole enzyme, next was tiglyl coenzyme A, Vmax = 61 x 10(3) moles/min mole enzyme, and last was 3-methyl-crotonyl coenzyme A, Vmax = 2.3 x 10(3) moles/min mole enzyme. Enzyme purified from butyrate cells had the same elution patterns during column chromatography and catalytic properties as the enzyme from isoleucine cells. These data support the conclusion that a single enzyme in P. putida is responsible for the hydration of both tiglyl coenzyme A and crotonyl coenzyme A. More... »

PAGES

99-108

Journal

TITLE

Archives of Microbiology

ISSUE

1

VOLUME

117

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00689358

DOI

http://dx.doi.org/10.1007/bf00689358

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1028103277

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/678016


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