PMID- 10652340
OWN - NLM
STAT- MEDLINE
DCOM- 20000302
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 275
IP  - 5
DP  - 2000 Feb 4
TI  - Purification and characterization of a neutral ceramidase from mouse liver. A
      single protein catalyzes the reversible reaction in which ceramide is both
      hydrolyzed and synthesized.
PG  - 3462-8
AB  - We report here a novel ceramidase that was purified more than 150, 000-fold from 
      the membrane fraction of mouse liver. The enzyme was a monomeric polypeptide
      having a molecular mass of 94 kDa and was highly glycosylated with N-glycans. The
      amino acid sequence of a fragment obtained from the purified enzyme was
      homologous to those deduced from the genes encoding an alkaline ceramidase of
      Pseudomonas aeruginosa and a hypotheical protein of the slime mold Dictyostelium 
      discoideum. However, no significant sequence similarities were found in other
      known functional proteins including acid ceramidases of humans and mice. The
      enzyme hydrolyzed various N-acylsphingosines but not galactosylceramide,
      sulfatide, GM1a, or sphingomyelin. The enzyme exhibited the highest activity
      around pH 7.5 and was thus identified as a type of neutral ceramidase. The
      apparent K(m) and V(max) values for C12-4-nitrobenzo-2-oxa-1, 3-diazole-ceramide 
      and C16-(14)C-ceramide were 22.3 microM and 29.1 micromol/min/mg and 72.4 microM 
      and 3.6 micromol/min/mg, respectively. This study also clearly demonstrated that 
      the purified 94-kDa ceramidase catalyzed the condensation of fatty acid to
      sphingosine to generate ceramide, but did not catalyze acyl-CoA-dependent
      acyl-transfer reaction.
FAU - Tani, M
AU  - Tani M
AD  - Department of Bioscience, Division of Bioresource and Bioenvironmental Sciences, 
      Graduate School Kyushu University, 6-10-1, Hakozaki, Higashi-ku, Fukuoka
      812-8581, Shiga 520-2134, Japan.
FAU - Okino, N
AU  - Okino N
FAU - Mitsutake, S
AU  - Mitsutake S
FAU - Tanigawa, T
AU  - Tanigawa T
FAU - Izu, H
AU  - Izu H
FAU - Ito, M
AU  - Ito M
LA  - eng
SI  - GENBANK/U82513
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Ceramides)
RN  - EC 3.5.- (Amidohydrolases)
RN  - EC 3.5.1.23 (ACER1 protein, human)
RN  - EC 3.5.1.23 (ACER2 protein, human)
RN  - EC 3.5.1.23 (ASAH2 protein, human)
RN  - EC 3.5.1.23 (Acer1 protein, mouse)
RN  - EC 3.5.1.23 (Alkaline Ceramidase)
RN  - EC 3.5.1.23 (Asah2 protein, mouse)
RN  - EC 3.5.1.23 (Ceramidases)
RN  - EC 3.5.1.23 (Neutral Ceramidase)
SB  - IM
MH  - Alkaline Ceramidase
MH  - Amidohydrolases/genetics/*isolation & purification/*metabolism
MH  - Amino Acid Sequence
MH  - Animals
MH  - Ceramidases
MH  - Ceramides/*metabolism
MH  - Enzyme Stability
MH  - Female
MH  - Hydrolysis
MH  - Liver/*enzymology
MH  - Mice
MH  - Molecular Sequence Data
MH  - Neutral Ceramidase
MH  - Sequence Alignment
MH  - Substrate Specificity
EDAT- 2000/02/01 09:00
MHDA- 2000/03/04 09:00
CRDT- 2000/02/01 09:00
PHST- 2000/02/01 09:00 [pubmed]
PHST- 2000/03/04 09:00 [medline]
PHST- 2000/02/01 09:00 [entrez]
AID - 10.1074/jbc.275.5.3462 [doi]
PST - ppublish
SO  - J Biol Chem. 2000 Feb 4;275(5):3462-8. doi: 10.1074/jbc.275.5.3462.