Search results for PISD

Showing 5 results out of 5

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Species

Types

Compartments

Search properties

Protein (2 results from a total of 2)

Identifier: R-HSA-1500670
Species: Homo sapiens
Compartment: mitochondrial inner membrane
Primary external reference: UniProt: PISD: Q9UG56
Identifier: R-HSA-1500671
Species: Homo sapiens
Compartment: mitochondrial inner membrane
Primary external reference: UniProt: Q9UG56

Reaction (1 results from a total of 1)

Identifier: R-HSA-1483212
Species: Homo sapiens
Compartment: mitochondrial inner membrane, mitochondrial matrix
At the inner mitochondrial (IM) membrane, phosphatidylserine decarboxylase proenzyme (heterodimer of two chains from the same protein) (PISD) decarboxylates phosphatidylserine (PS) to phosphatidylethanolamine (PE). This event has been inferred from rats and limited data for a human PISD (Forbes et al. 2007).

Complex (1 results from a total of 1)

Identifier: R-HSA-1500656
Species: Homo sapiens
Compartment: mitochondrial inner membrane

Pathway (1 results from a total of 1)

Identifier: R-HSA-1483213
Species: Homo sapiens
De novo (Kennedy pathway) synthesis of phosphatidylethanolamine (PE) involves phosphorylation of ethanolamine (ETA) to phosphoethanolamine (PETA) followed by condensing with cytidine triphosphate (CTP) to form CDP-ethanolamine (CDP-ETA). Diacylglycerol (DAG) and CDP-ETA together then form PE. Alternatively, PE is formed when phosphatidylserine (PS) is decarboxylated by phosphatidylserine decarboxylase proenzyme (PISD) (Henneberry et al. 2002, Vance 1991, Vance 1990).
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