Structural Insights into the Enzymatic Mechanism of Serine Palmitoyltransferase from Sphingobacterium multivorum-Reference-Cited by-同舟云学术

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Structural Insights into the Enzymatic Mechanism of Serine Palmitoyltransferase from Sphingobacterium multivorum

Published:2009-06-29 Issue:4 Volume:146 Page:549-562
ISSN:0021-924X
Container-title:Journal of Biochemistry
language:en
Short-container-title:Journal of Biochemistry

Author:

Ikushiro H.,Islam M. M.,Okamoto A.,Hoseki J.,Murakawa T.,Fujii S.,Miyahara I.,Hayashi H.

Publisher

Oxford University Press (OUP)

Subject

Molecular Biology,Biochemistry,General Medicine

Link

http://academic.oup.com/jb/article-pdf/146/4/549/6249808/mvp100.pdf

Reference45 articles.

1. Omega-O-acylceramide, a lipid essential for mammalian survival

2. The complex life of simple sphingolipids

3. Sphingosine-1-phosphate: an enigmatic signalling lipid

5. Serine palmitoyltransferase, a key enzyme of sphingolipid metabolism

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1. The structure of the Orm2-containing serine palmitoyltransferase complex reveals distinct inhibitory potentials of yeast Orm proteins;Cell Reports;2024-08

2. Regulation of cellular and systemic sphingolipid homeostasis;Nature Reviews Molecular Cell Biology;2024-06-18

3. Rational Engineering of a Thermostable α-Oxoamine Synthase Biocatalyst Expands the Substrate Scope and Synthetic Applicability;2024-05-14

4. Structural and mechanistic investigations on C C bond forming α-oxoamine synthase allowing L-glutamate as substrate;International Journal of Biological Macromolecules;2024-05

5. Racemization of the substrate and product by serine palmitoyltransferase from Sphingobacterium multivorum yields two enantiomers of the product from d-serine;Journal of Biological Chemistry;2024-03

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