PMID- 10064901
OWN - NLM
STAT- MEDLINE
DCOM- 19990413
LR  - 20190610
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1437
IP  - 2
DP  - 1999 Feb 25
TI  - Sequence, expression in Escherichia coli, and characterization of
      lysophospholipase II.
PG  - 182-93
AB  - Here we report the sequence, expression in Escherichia coli cells, and
      characterization of a new small-form lysophospholipase named lysophospholipase II
      from mouse embryo. The cDNA clone was found and identified among mouse expressed 
      sequence tags in the database search for the homologue of lysophospholipase I
      previously cloned from rat liver (H. Sugimoto et al., J. Biol. Chem. 271 (1996)
      7705-7711). The predicted amino acids sequence contained 231 residues with a
      calculated molecular weight of 24794, and showed 64% identity to that of
      lysophospholipase I with the Gly-X-Ser-X-Gly esterase/lipase consensus. The lacZ 
      fusion protein expressed in E. coli cells exhibited lysophospholipase activity
      and reacted with antibody raised against previously purified pig gastric
      lysophospholipase II (H. Sunaga et al., Biochem. J. 308 (1995) 551-557), but not 
      with antibody against rat liver lysophospholipase I. The expressed enzyme was
      purified to a specific activity of 0.15 micromol/min per mg by DEAE-Sepharose
      A-500 chromatography. The enzyme preferentially utilized zwitterionic
      lysophospholipids in the order of
      lysophosphatidylcholine>lysophosphatidylethanolamine, but poorly acidic
      lysophospholipids, such as lysophosphatidylserine, lysophosphatidylinositol, and 
      lysophosphatidic acid. Not only the 1-acyl isomer, but also the 2-acyl isomer
      were deacylated. Northern blot analysis and reverse transcription-polymerase
      chain reaction revealed that lysophospholipase II transcript as well as
      lysophospholipase I transcript was widely distributed in mouse tissues.
FAU - Toyoda, T
AU  - Toyoda T
AD  - Department of Biochemistry, Gunma University School of Medicine, 3-39-22
      Showamachi, Maebashi, Gunma 371-8511, Japan.
FAU - Sugimoto, H
AU  - Sugimoto H
FAU - Yamashita, S
AU  - Yamashita S
LA  - eng
SI  - GENBANK/AB009653
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (DNA, Complementary)
RN  - 0 (RNA, Messenger)
RN  - EC 3.1.1.5 (Lysophospholipase)
RN  - EC 3.1.2.- (Lypla2 protein, mouse)
RN  - EC 3.1.2.- (Thiolester Hydrolases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Consensus Sequence
MH  - DNA, Complementary/chemistry
MH  - Escherichia coli/genetics/metabolism
MH  - Gene Expression
MH  - Lysophospholipase/*biosynthesis/chemistry/genetics
MH  - Mice
MH  - Molecular Sequence Data
MH  - RNA, Messenger/analysis
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Sequence Homology, Amino Acid
MH  - Substrate Specificity
MH  - Thiolester Hydrolases
EDAT- 1999/03/05 00:00
MHDA- 1999/03/05 00:01
CRDT- 1999/03/05 00:00
PHST- 1999/03/05 00:00 [pubmed]
PHST- 1999/03/05 00:01 [medline]
PHST- 1999/03/05 00:00 [entrez]
AID - S1388-1981(99)00007-4 [pii]
AID - 10.1016/s1388-1981(99)00007-4 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 1999 Feb 25;1437(2):182-93. doi:
      10.1016/s1388-1981(99)00007-4.