Abstract
The recent identification of cDNA clones for phospholipase D has opened the door to new types of investigations into its structure and regulation. PLD activity has been found to be encoded by at least two different genes that contain catalytic domains that relate their mechanism of action to phosphodiesterases. In vivo roles for PLD suggest that it may be important for multiples steps in regulated secretion and membrane biogenesis.
Publication types
-
Research Support, U.S. Gov't, P.H.S.
-
Review
MeSH terms
-
Amino Acid Sequence
-
Animals
-
Cloning, Molecular
-
DNA, Complementary
-
Gene Expression Regulation, Enzymologic*
-
Humans
-
Molecular Sequence Data
-
Phospholipase D / chemistry*
-
Phospholipase D / genetics*
-
Phospholipase D / metabolism
-
Phosphoric Diester Hydrolases / metabolism
-
Protein Conformation
-
Recombinant Proteins / chemistry
-
Recombinant Proteins / metabolism
-
Sequence Alignment
-
Sequence Homology, Amino Acid
Substances
-
DNA, Complementary
-
Recombinant Proteins
-
Phosphoric Diester Hydrolases
-
Phospholipase D