PMID- 10585463
OWN - NLM
STAT- MEDLINE
DCOM- 20000113
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 50
DP  - 1999 Dec 10
TI  - Cloning, expression, and cellular localization of a human prenylcysteine lyase.
PG  - 35802-8
AB  - Prenylated proteins contain either a 15-carbon farnesyl or 20-carbon
      geranylgeranyl isoprenoid covalently attached to cysteine residues at or near
      their C terminus. These proteins constitute up to 2% of total cellular protein in
      eukaryotic cells. The degradation of prenylated proteins raises a metabolic
      challenge to the cell, because the thioether bond of the modified cysteine is
      quite stable. We recently identified and isolated an enzyme termed prenylcysteine
      lyase that cleaves the prenylcysteine to free cysteine and an isoprenoid product 
      (Zhang, L., Tschantz, W. R., and Casey, P. J. (1997) J. Biol. Chem. 272,
      23354-23359). To facilitate the molecular characterization of this enzyme, its
      cloning was undertaken. Overlapping cDNA clones encoding the complete coding
      sequence of this enzyme were obtained from a human cDNA library. The open reading
      frame of the gene encoding prenylcysteine lyase is 1515 base pairs and has a
      nearly ubiquitous expression pattern with a message size of 6 kilobase pairs.
      Recombinant prenylcysteine lyase was produced in a baculovirus-Sf9 expression
      system. Analysis of both the recombinant and native enzyme revealed that the
      enzyme is glycosylated and contains a signal peptide that is cleaved during
      processing. Additionally, the subcellular localization of this enzyme was
      determined to be lysosomal. These findings strengthen the notion that
      prenylcysteine lyase plays an important role in the final step in the degradation
      of prenylated proteins and will allow further physiological and biochemical
      characterization of this enzyme.
FAU - Tschantz, W R
AU  - Tschantz WR
AD  - Department of Pharmacology, Duke University Medical Center, Durham, North
      Carolina 27710, USA.
FAU - Zhang, L
AU  - Zhang L
FAU - Casey, P J
AU  - Casey PJ
LA  - eng
SI  - GENBANK/AF181490
GR  - GM18069/GM/NIGMS NIH HHS/United States
GR  - GM46372/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (DNA, Complementary)
RN  - 0 (Peptide Fragments)
RN  - 0 (Recombinant Proteins)
RN  - EC 1.8.3.5 (PCYOX1 protein, human)
RN  - EC 1.8.3.5 (prenylcysteine lyase)
RN  - EC 4.4.- (Carbon-Sulfur Lyases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Base Sequence
MH  - Brain/enzymology
MH  - Carbon-Sulfur Lyases/chemistry/*genetics/*metabolism
MH  - Cloning, Molecular
MH  - DNA, Complementary
MH  - *Gene Expression Regulation, Enzymologic
MH  - Glycosylation
MH  - Humans
MH  - Kinetics
MH  - Molecular Sequence Data
MH  - Organ Specificity
MH  - Peptide Fragments/chemistry
MH  - Protein Biosynthesis
MH  - Recombinant Proteins/chemistry/metabolism
MH  - Reticulocytes/metabolism
EDAT- 1999/12/10 00:00
MHDA- 1999/12/10 00:01
CRDT- 1999/12/10 00:00
PHST- 1999/12/10 00:00 [pubmed]
PHST- 1999/12/10 00:01 [medline]
PHST- 1999/12/10 00:00 [entrez]
AID - 10.1074/jbc.274.50.35802 [doi]
AID - S0021-9258(19)53314-2 [pii]
PST - ppublish
SO  - J Biol Chem. 1999 Dec 10;274(50):35802-8. doi: 10.1074/jbc.274.50.35802.