PMID- 10220586
OWN - NLM
STAT- MEDLINE
DCOM- 19990811
LR  - 20190513
IS  - 0021-924X (Print)
IS  - 0021-924X (Linking)
VI  - 125
IP  - 5
DP  - 1999 May
TI  - Molecular cloning of adipocyte-derived leucine aminopeptidase highly related to
      placental leucine aminopeptidase/oxytocinase.
PG  - 931-8
AB  - In the current study, we report the cloning and initial characterization of a
      novel human cytosolic aminopeptidase named adipocyte-derived leucine
      aminopeptidase (A-LAP). The sequence encodes a 941-amino acid protein with
      significant homology (43%) to placental leucine aminopeptidase
      (P-LAP)/oxytocinase. The predicted A-LAP contains the HEXXH(X)18E consensus
      sequence, which is characteristic of the M1 family of zinc-metallopeptidases.
      Although the deduced sequence contains a hydrophobic region near the N-terminus, 
      the enzyme localized mainly in cytoplasm when expressed in COS-7 cells. Northern 
      blot analysis revealed that A-LAP was expressed in all the tissues tested, some
      of which expressed at least three forms of mRNA, suggesting that the regulation
      of the gene expression is complex. When aminopeptidase activity of A-LAP was
      measured with various synthetic substrates, the enzyme revealed a preference for 
      leucine, establishing that A-LAP is a novel leucine aminopeptidase with
      restricted substrate specificity. The identification of A-LAP, which reveals
      strong homology to P-LAP, might lead to the definition of a new subfamily of
      zinc-containing aminopeptidases belonging to the M1 family of metallopeptidases.
FAU - Hattori, A
AU  - Hattori A
AD  - Laboratory of Cellular Biochemistry, The Institute of Physical and Chemical
      Research (RIKEN), Wako, Saitama, 351-0198, Japan.
FAU - Matsumoto, H
AU  - Matsumoto H
FAU - Mizutani, S
AU  - Mizutani S
FAU - Tsujimoto, M
AU  - Tsujimoto M
LA  - eng
SI  - GENBANK/AF106037
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Biochem
JT  - Journal of biochemistry
JID - 0376600
RN  - 0 (DNA, Complementary)
RN  - EC 3.4.11.1 (Leucyl Aminopeptidase)
RN  - EC 3.4.11.3 (Cystinyl Aminopeptidase)
SB  - IM
MH  - Adipocytes/*enzymology
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Blotting, Northern
MH  - COS Cells
MH  - Cloning, Molecular
MH  - Cystinyl Aminopeptidase/*genetics
MH  - DNA, Complementary
MH  - Humans
MH  - Leucyl Aminopeptidase/*genetics
MH  - Molecular Sequence Data
MH  - Placenta/*enzymology
MH  - Sequence Homology, Amino Acid
MH  - Subcellular Fractions/enzymology
EDAT- 1999/04/30 00:00
MHDA- 1999/04/30 00:01
CRDT- 1999/04/30 00:00
PHST- 1999/04/30 00:00 [pubmed]
PHST- 1999/04/30 00:01 [medline]
PHST- 1999/04/30 00:00 [entrez]
AID - 10.1093/oxfordjournals.jbchem.a022371 [doi]
PST - ppublish
SO  - J Biochem. 1999 May;125(5):931-8. doi: 10.1093/oxfordjournals.jbchem.a022371.