Abstract
The initial step in the fermentation of leucine to acetate, isobutyrate, and ammonia by Clostridium sporogenes is the B12 coenzyme-dependent conversion of alpha-leucine to beta-leucine (3-amino-4-methylpentanoate). The amino group migration reaction, catalyzed by leucine 2,3-aminomutase, is reversible and is inhibited by intrinsic factor. The enzyme activity has been found in several clostridia, in rat, sheep, rhesus, and African green monkey livers, and in human leukocytes.
Highlights
The initial step in the fermentation of leucine to acetate, isobutyrate, and ammonia by Clostridium sporogenes is the B, coenzyme-dependent conversion of oc-leucine to /?-leucine (3.amino-4-methylpentanoate)
Identification of isobutyric acid and P-ketoisocaproic acid as products of leucine metabolism suggested that the primary attack on the amino acid substrate might involve an isomerization to form @-leucine
The discovery that isobutyric acid is a major end product of leucine metabolism by C. sporogenes suggested that a metabolic pathway other than the known one might be involved
Summary
Cellular Material-A spore-forming obligate anaerobe was isolated from mud from the Amazon basin of Ecuador [1] by the enrichment of the culture with L-leucine. The benzene was added to the oily upper layer and this solution was washed with 250 ml of. Measurement of a-leucine--a-Leucine and other free a-amino acids were measured by the method of Spackman et al [11] in a. Measurenent of /3-Leucine-&Leucine does not react with ninhydrin to give a colored product in the standard ninhydrin methods and cannot be measured in the amino acid analyzer. @-Leucine separates from ol-leucine on silica gel thin layer chromatograms developed in lbutanol/acetic acid/water (5/l/2) with an R, of 0.66 for 8-leucine and.
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
