Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/194448
Type: Artigo de periódico
Title: Lysine Degradation Through The Saccharopine Pathway In Mammals: Involvement Of Both Bifunctional And Monofunctional Lysine-degrading Enzymes In Mouse.
Author: Papes, F
Kemper, E L
Cord-Neto, G
Langone, F
Arruda, P
Abstract: Lysine-oxoglutarate reductase and saccharopine dehydrogenase are enzymic activities that catalyse the first two steps of lysine degradation through the saccharopine pathway in upper eukaryotes. This paper describes the isolation and characterization of a cDNA clone encoding a bifunctional enzyme bearing domains corresponding to these two enzymic activities. We partly purified those activities from mouse liver and showed for the first time that both a bifunctional lysine-oxoglutarate reductase/saccharopine dehydrogenase and a monofunctional saccharopine dehydrogenase are likely to be present in this organ. Northern analyses indicate the existence of two mRNA species in liver and kidney. The longest molecule, 3.4 kb in size, corresponds to the isolated cDNA and encodes the bifunctional enzyme. The 2.4 kb short transcript probably codes for the monofunctional dehydrogenase. Sequence analyses show that the bifunctional enzyme is likely to be a mitochondrial protein. Furthermore, enzymic and expression analyses suggest that lysine-oxoglutarate reductase/saccharopine dehydrogenase levels increase in livers of mice under starvation. Lysine-injected mice also show an increase in lysine-oxoglutarate reductase and saccharopine dehydrogenase levels.
Subject: Amino Acid Sequence
Animals
Gene Expression Regulation, Enzymologic
Gene Library
Kidney
Liver
Lysine
Mice
Molecular Sequence Data
Multienzyme Complexes
Saccharopine Dehydrogenases
Sequence Homology, Amino Acid
Starvation
Tissue Distribution
Rights: fechado
Identifier DOI: 
Address: http://www.ncbi.nlm.nih.gov/pubmed/10567240
Date Issue: 1999
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

Files in This Item:
File SizeFormat 
pmed_10567240.pdf300.85 kBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.