Unknown

Dataset Information

0

Biosynthesis of long chain base in sphingolipids in animals, plants and fungi.


ABSTRACT: Long chain base (LCB) is a unique building block found in sphingolipids. The initial step of LCB biosynthesis stems from serine:palmitoyl-CoA transferase enzyme, producing 3-ketodihydrosphingosine with multiple regulatory proteins including small subunit SPT a/b and orosomucoid-like protein1-3. 3-Ketodihydrosphingosine reductase and sphingolipid ?4-desaturase, both of them poorly characterized mammalian enzymes, play key roles for neurological homeostasis based on their pathogenic mutation in humans. Ceramide synthase in mammals has six isoforms with distinct phenotype in each knockout mouse. In plants and fungi, sphingolipids also contain phytosphingosine due to sphingolipid C4-hydroxylase. In contrast to previous notion that dietary intake might be its major route in animals, emerging evidences suggested that phytosphingosine biosynthesis does occur in some tissues such as the skin by mammalian C4-hydroxylase activity of the DEGS2 gene. This short review summarizes LCB biosynthesis with their associating metabolic pathways in animals, plants and fungi.

SUBMITTER: Mashima R 

PROVIDER: S-EPMC6920741 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

Biosynthesis of long chain base in sphingolipids in animals, plants and fungi.

Mashima Ryuichi R   Okuyama Torayuki T   Ohira Mari M  

Future science OA 20191114 1


Long chain base (LCB) is a unique building block found in sphingolipids. The initial step of LCB biosynthesis stems from serine:palmitoyl-CoA transferase enzyme, producing 3-ketodihydrosphingosine with multiple regulatory proteins including small subunit SPT a/b and orosomucoid-like protein1-3. 3-Ketodihydrosphingosine reductase and sphingolipid Δ4-desaturase, both of them poorly characterized mammalian enzymes, play key roles for neurological homeostasis based on their pathogenic mutation in hu  ...[more]

Similar Datasets

| S-EPMC208092 | biostudies-other
| S-EPMC3706215 | biostudies-literature
| S-EPMC2174859 | biostudies-literature
| S-EPMC1132344 | biostudies-other
| S-EPMC9240600 | biostudies-literature
| S-EPMC2941185 | biostudies-literature
| S-EPMC2884541 | biostudies-literature
| S-EPMC1698682 | biostudies-literature
| S-EPMC5913725 | biostudies-literature
| S-EPMC5817892 | biostudies-literature