BRENDA - Enzyme Database

Phosphatidic acid (PA)-preferring phospholipase A1 regulates mitochondrial dynamics

Baba, T.; Kashiwagi, Y.; Arimitsu, N.; Kogure, T.; Edo, A.; Maruyama, T.; Nakao, K.; Nakanishi, H.; Kinoshita, M.; Frohman, M.A.; Yamamoto, A.; Tani, K.; J. Biol. Chem. 289, 11497-11511 (2014)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
3.1.1.32
expression of FLAG-tagged wild-type and mutant enzymes in HeLa cells and in siRNA-treated knockout mutant HeLa cells. Upon overexpression of wild-type enzyme, the tubular structures become fragmented, expression of the mutant S537A has no effect
Homo sapiens
Engineering
EC Number
Amino acid exchange
Commentary
Organism
3.1.1.32
additional information
construction of enzyme knockout mutant HeLa cells by treatment with specific siRNA, phenotype, overview
Homo sapiens
3.1.1.32
additional information
generation of phosphatidic acid-preferring phospholipase A1 knock-out mice using targeting vector clone PGS00049_B_D06 and specific siRNA, phenotype, overview
Mus musculus
3.1.1.32
S537A
site-directed mutagenesis, inactive mutant
Homo sapiens
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
3.1.1.32
intracellular
-
Homo sapiens
5622
-
3.1.1.32
intracellular
-
Mus musculus
5622
-
3.1.1.32
mitochondrion
-
Homo sapiens
5739
-
3.1.1.32
mitochondrion
-
Mus musculus
5739
-
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3.1.1.32
phosphatidic acid + H2O
Mus musculus
-
2-acyl-lysophosphatidic acid + a carboxylate
-
-
?
3.1.1.32
phosphatidic acid + H2O
Homo sapiens
-
2-acyl-lysophosphatidic acid + a carboxylate
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
3.1.1.32
Homo sapiens
-
-
-
3.1.1.32
Mus musculus
-
-
-
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
3.1.1.32
brain
high expression level
Homo sapiens
-
3.1.1.32
caput epididymis
-
Mus musculus
-
3.1.1.32
cauda epididymis
-
Mus musculus
-
3.1.1.32
HeLa cell
-
Homo sapiens
-
3.1.1.32
spermatozoon
-
Mus musculus
-
3.1.1.32
testis
high expression level
Homo sapiens
-
3.1.1.32
testis
high expression level
Mus musculus
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.1.1.32
phosphatidic acid + H2O
-
730037
Mus musculus
2-acyl-lysophosphatidic acid + a carboxylate
-
-
-
?
3.1.1.32
phosphatidic acid + H2O
-
730037
Homo sapiens
2-acyl-lysophosphatidic acid + a carboxylate
-
-
-
?
3.1.1.32
phosphatidic acid + H2O
preferred substrate in vitro
730037
Mus musculus
2-acyl-lysophosphatidic acid + a carboxylate
-
-
-
?
3.1.1.32
phosphatidic acid + H2O
preferred substrate in vitro
730037
Homo sapiens
2-acyl-lysophosphatidic acid + a carboxylate
-
-
-
?
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
3.1.1.32
expression of FLAG-tagged wild-type and mutant enzymes in HeLa cells and in siRNA-treated knockout mutant HeLa cells. Upon overexpression of wild-type enzyme, the tubular structures become fragmented, expression of the mutant S537A has no effect
Homo sapiens
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
3.1.1.32
additional information
construction of enzyme knockout mutant HeLa cells by treatment with specific siRNA, phenotype, overview
Homo sapiens
3.1.1.32
additional information
generation of phosphatidic acid-preferring phospholipase A1 knock-out mice using targeting vector clone PGS00049_B_D06 and specific siRNA, phenotype, overview
Mus musculus
3.1.1.32
S537A
site-directed mutagenesis, inactive mutant
Homo sapiens
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
3.1.1.32
intracellular
-
Homo sapiens
5622
-
3.1.1.32
intracellular
-
Mus musculus
5622
-
3.1.1.32
mitochondrion
-
Homo sapiens
5739
-
3.1.1.32
mitochondrion
-
Mus musculus
5739
-
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3.1.1.32
phosphatidic acid + H2O
Mus musculus
-
2-acyl-lysophosphatidic acid + a carboxylate
-
-
?
3.1.1.32
phosphatidic acid + H2O
Homo sapiens
-
2-acyl-lysophosphatidic acid + a carboxylate
-
-
?
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
3.1.1.32
brain
high expression level
Homo sapiens
-
3.1.1.32
caput epididymis
-
Mus musculus
-
3.1.1.32
cauda epididymis
-
Mus musculus
-
3.1.1.32
HeLa cell
-
Homo sapiens
-
3.1.1.32
spermatozoon
-
Mus musculus
-
3.1.1.32
testis
high expression level
Homo sapiens
-
3.1.1.32
testis
high expression level
Mus musculus
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.1.1.32
phosphatidic acid + H2O
-
730037
Mus musculus
2-acyl-lysophosphatidic acid + a carboxylate
-
-
-
?
3.1.1.32
phosphatidic acid + H2O
-
730037
Homo sapiens
2-acyl-lysophosphatidic acid + a carboxylate
-
-
-
?
3.1.1.32
phosphatidic acid + H2O
preferred substrate in vitro
730037
Mus musculus
2-acyl-lysophosphatidic acid + a carboxylate
-
-
-
?
3.1.1.32
phosphatidic acid + H2O
preferred substrate in vitro
730037
Homo sapiens
2-acyl-lysophosphatidic acid + a carboxylate
-
-
-
?
General Information
EC Number
General Information
Commentary
Organism
3.1.1.32
malfunction
phosphatidic acid-preferring phospholipase A1 depletion causes mitochondrial elongation, leading to a loss of motility
Homo sapiens
3.1.1.32
malfunction
phosphatidic acid-preferring phospholipase A1 depletion causes mitochondrial elongation. Enzyme knock-out mice have a defect in sperm formation, spermatozoa from PA-PLA1-/- mice possess an annulus that is not attached to the mitochondrial sheath, whereas that in control mice is attached. In enzyme-deficient sperm, the mitochondrial structure is disorganized, and an abnormal gap structure exists between the middle and principal pieces.A flagellum is bent at that position, leading to a loss of motility
Mus musculus
3.1.1.32
physiological function
the phosphatidic acid-preferring phospholipase A1 regulates mitochondrial dynamics. When ectopically expressed in HeLa cells, it induces mitochondrial fragmentation, whereas its depletion causes mitochondrial elongation. The effects of the enzyme on mitochondrial morphology appear to counteract those of MitoPLD, a mitochondrion-localized phospholipase D that produces phosphatidic acid from cardiolipin
Homo sapiens
3.1.1.32
physiological function
the phosphatidic acid-preferring phospholipase A1 regulates mitochondrial dynamics
Mus musculus
General Information (protein specific)
EC Number
General Information
Commentary
Organism
3.1.1.32
malfunction
phosphatidic acid-preferring phospholipase A1 depletion causes mitochondrial elongation, leading to a loss of motility
Homo sapiens
3.1.1.32
malfunction
phosphatidic acid-preferring phospholipase A1 depletion causes mitochondrial elongation. Enzyme knock-out mice have a defect in sperm formation, spermatozoa from PA-PLA1-/- mice possess an annulus that is not attached to the mitochondrial sheath, whereas that in control mice is attached. In enzyme-deficient sperm, the mitochondrial structure is disorganized, and an abnormal gap structure exists between the middle and principal pieces.A flagellum is bent at that position, leading to a loss of motility
Mus musculus
3.1.1.32
physiological function
the phosphatidic acid-preferring phospholipase A1 regulates mitochondrial dynamics. When ectopically expressed in HeLa cells, it induces mitochondrial fragmentation, whereas its depletion causes mitochondrial elongation. The effects of the enzyme on mitochondrial morphology appear to counteract those of MitoPLD, a mitochondrion-localized phospholipase D that produces phosphatidic acid from cardiolipin
Homo sapiens
3.1.1.32
physiological function
the phosphatidic acid-preferring phospholipase A1 regulates mitochondrial dynamics
Mus musculus