Kicking off sphingolipid biosynthesis: structures of the serine palmitoyltransferase complex

Structures of the human serine palmitoyltransferase complex reveal the overall assembly, regulatory mechanisms and substrate selectivity of this key enzyme in sphingolipid synthesis.

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Bibliographische Detailangaben
Veröffentlicht in:	Nature structural & molecular biology 2021-03, Vol.28 (3), p.229-231
1. Verfasser:	Wattenberg, Binks W.
Format:	Artikel
Sprache:	eng
Schlagworte:	101/28 631/45/287/1192 631/535/1258/1259 Binding sites Biochemistry Biological Microscopy Biomedical and Life Sciences Biosynthesis Carbon Endoplasmic reticulum Enzymes Fatty acids Humans Hydrocarbons Life Sciences Lipid research Lipids Mammals Membrane Biology Models, Molecular Molecular biology News & Views news-and-views Palmitoyltransferase Physiological aspects Protein Structure Proteins Regulation Regulatory mechanisms (biology) Selectivity Serine Serine C-Palmitoyltransferase - chemistry Serine C-Palmitoyltransferase - metabolism Serine palmitoyltransferase Sphingolipids Sphingolipids - biosynthesis Sphingolipids - metabolism Structure Substrates Synthesis Transferases
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Beschreibung
Zusammenfassung:	Structures of the human serine palmitoyltransferase complex reveal the overall assembly, regulatory mechanisms and substrate selectivity of this key enzyme in sphingolipid synthesis.
ISSN:	1545-9993 1545-9985
DOI:	10.1038/s41594-021-00562-0