PMID- 10567240
OWN - NLM
STAT- MEDLINE
DCOM- 20000211
LR  - 20181113
IS  - 0264-6021 (Print)
IS  - 0264-6021 (Linking)
VI  - 344 Pt 2
DP  - 1999 Dec 1
TI  - Lysine degradation through the saccharopine pathway in mammals: involvement of
      both bifunctional and monofunctional lysine-degrading enzymes in mouse.
PG  - 555-63
AB  - 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.
FAU - Papes, F
AU  - Papes F
AD  - Centro de Biologia Molecular e Engenharia Genetica, Universidade Estadual de
      Campinas, Campinas, CEP 13083-970, SP, Brasil.
FAU - Kemper, E L
AU  - Kemper EL
FAU - Cord-Neto, G
AU  - Cord-Neto G
FAU - Langone, F
AU  - Langone F
FAU - Arruda, P
AU  - Arruda P
LA  - eng
SI  - GENBANK/AF003551
SI  - GENBANK/AJ224761
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Biochem J
JT  - The Biochemical journal
JID - 2984726R
RN  - 0 (Multienzyme Complexes)
RN  - EC 1.5.1.- (Saccharopine Dehydrogenases)
RN  - K3Z4F929H6 (Lysine)
RN  - WBQ73O8W32 (saccharopine)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Gene Expression Regulation, Enzymologic
MH  - Gene Library
MH  - Kidney/enzymology
MH  - Liver/enzymology
MH  - Lysine/*analogs & derivatives/*metabolism
MH  - Mice
MH  - Molecular Sequence Data
MH  - Multienzyme Complexes/genetics/isolation & purification/*metabolism
MH  - Saccharopine Dehydrogenases/genetics/isolation & purification/*metabolism
MH  - Sequence Homology, Amino Acid
MH  - Starvation/metabolism
MH  - Tissue Distribution
PMC - PMC1220675
EDAT- 1999/11/24 09:00
MHDA- 2000/02/19 09:00
CRDT- 1999/11/24 09:00
PHST- 1999/11/24 09:00 [pubmed]
PHST- 2000/02/19 09:00 [medline]
PHST- 1999/11/24 09:00 [entrez]
PST - ppublish
SO  - Biochem J. 1999 Dec 1;344 Pt 2:555-63.