The human serine palmitoyltransferase (SPT) complex; specificity, structure, regulation and inhibition.

Campopiano, Dominic (Principal Investigator)

School of Chemistry

Status	Finished
Effective start/end date	30/01/15 → 29/01/18

Funding

BBSRC: £704,002.00

6 Article

BioWF: A naturally‐fused, di‐domain biocatalyst from biotin biosynthesis displays an unexpectedly broad substrate scope
Richardson, S. M., Harrison, P. J., Herrera, M. A., Wang, M., Verez, R., Ortiz, G. P. & Campopiano, D. J., 13 Jun 2022, (E-pub ahead of print) In: ChemBioChem.
Research output: Contribution to journal › Article › peer-review

Open Access
File
Use of isotopically labeled substrates reveals kinetic differences between human and bacterial serine palmitoyltransferase
Harrison, P. J., Gable, K., Somashekarappa, N., Kelly, V., Clarke, D. J., Naismith, J. H., Dunn, T. M. & Campopiano, D. J., 21 Feb 2019, (E-pub ahead of print) In: Journal of lipid research. 60, 5, p. 953-962
Research output: Contribution to journal › Article › peer-review

Open Access
File
Sphingolipid biosynthesis in man and microbes
Harrison, P. J., Dunn, T. & Campopiano, D. J., 4 Jun 2018, (E-pub ahead of print) In: Natural product reports.
Research output: Contribution to journal › Article › peer-review

Open Access
File

Use of Isotopically Labelled Substrates Reveals Kinetic Differences Between Human and Bacterial Serine Palmitoyltransferase
Harrison, P. (Creator), Clarke, D. (Creator), Kelly, V. (Creator) & Campopiano, D. (Creator), Edinburgh DataShare, 4 Mar 2019
DOI: 10.7488/ds/2503, http://www.jlr.org/content/early/2019/02/21/jlr.M089367.long
Dataset