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Literature summary for 3.1.1.47 extracted from

  • Gardner, A.A.; Reichert, E.C.; Alexander, T.S.; Topham, M.K.; Stafforini, D.M.
    Novel mechanism for regulation of plasma platelet-activating factor acetylhydrolase expression in mammalian cells (2010), Biochem. J., 428, 269-279.
    View publication on PubMed
Search for more literature for 3.1.1.47

Cloned(Commentary)

Cloned (Comment) Organism
expression of N- and C-FLAG-tagged wild-type human PAF-AH, expression of FLAG-tagged human wild-type PAF-AH and of the engineered PAF-AH mutant in Escherichia coli. A region located at the N-terminal end of PAF-AH regulates expression levels Mus musculus
expression of N- and C-FLAG-tagged wild-type mouse PAF-AH, expression of FLAG-tagged human wild-type PAF-AH and of the engineered PAF-AH mutant in Escherichia coli. A region located at the N-terminal end of PAF-AH regulates expression levels Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information replacement of human PAF-AH residues 42-100 with mouse PAF-AH amino acids 41-99, resulting in construct m41-99H, dramatically increases protein and enzymatic activity expression. Conversely, when mouse cDNA N-terminal residues are replaced with the equivalent human sequences, resulting in construct h42-100M, the levels of expression are significantly decreased Mus musculus
additional information replacement of human PAF-AH residues 42-100 with mouse PAF-AH amino acids 41-99, resulting in construct m41-99H, dramatically increases protein and enzymatic activity expression. Conversely, when mouse cDNA N-terminal residues are replaced with the equivalent human sequences, resulting in construct h42-100M, the levels of expression are significantly decreased Homo sapiens
N59Q site-directed mutagenesis, the mutant and wild-type mouse PAFAH expression levels are similar Mus musculus
N75Q site-directed mutagenesis, the mutant and wild-type mouse PAFAH expression levels are similar Mus musculus
S61P/P63S site-directed mutagenesis, the mutant and wild-type mouse PAFAH expression levels are similar Mus musculus

General Stability

General Stability Organism
human PAF-AH protein is rapidly degraded after cycloheximide treatment of cells, a large portion of immunoreactive precursors are inactive and short-lived Homo sapiens
mouse PAF-AH species displays remarkable stability, and enzymatic activity continues to increase after cycloheximide addition due to processing of inactive precursors to fully active protein Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular secreted enzyme Homo sapiens
-
-
extracellular secereted enzyme Mus musculus
-
-
intracellular
-
 Mus musculus 5622
-
intracellular
-
 Homo sapiens 5622
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Mus musculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
plasma
-
 Mus musculus
-
plasma
-
 Homo sapiens
-

Synonyms

Synonyms Comment Organism
PAF-acetylhydrolase
-
 Mus musculus
PAF-acetylhydrolase
-
 Homo sapiens
PAF-AH
-
 Mus musculus
PAF-AH
-
 Homo sapiens
plasma platelet-activating factor acetylhydrolase
-
 Mus musculus
plasma platelet-activating factor acetylhydrolase
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Mus musculus
30
-
 assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Mus musculus
7.5
-
 assay at Homo sapiens

General Information

General Information Comment Organism
additional information higher expression of mouse compared with human PAF-AH is not due to variations in catalytic efficiency. A region located at the N-terminal end of PAF-AH regulates expression levels, the degree of hydrophobicity and polarity of the N-terminal region correlates with the level of PAF-AH expression Mus musculus
additional information higher expression of mouse compared with human PAF-AH is not due to variations in catalytic efficiency. A region located at the N-terminal end of PAF-AH regulates expression levels, the degree of hydrophobicity and polarity of the N-terminal region correlates with the level of PAF-AH expression Homo sapiens