scispace - formally typeset
A

Antoni R. Slabas

Researcher at Durham University

Publications -  171
Citations -  7580

Antoni R. Slabas is an academic researcher from Durham University. The author has contributed to research in topics: Acyl carrier protein & Reductase. The author has an hindex of 49, co-authored 171 publications receiving 7194 citations. Previous affiliations of Antoni R. Slabas include University of London.

Papers
More filters
Journal ArticleDOI

Kinetic mechanism and order of substrate binding for sn-glycerol-3-phosphate acyltransferase from squash (Cucurbita moschata).

TL;DR: The kinetic mechanism of plastidial G3PAT from squash and the order of substrate binding using acyl‐acyl carrier protein (acyl‐ACP) substrates are reported and it is determined that the reaction will proceed with C4:0‐CoA, C6:0•CoA and C12:0-ACP substrates, allowing a wider choice of acyl groups for future co‐crystallisation studies.
Journal ArticleDOI

Components of complex lipid biosynthetic pathways in developing castor (Ricinus communis) seeds identified by MudPIT analysis of enriched endoplasmic reticulum.

TL;DR: To identify castor oil-biosynthetic enzymes and inform strategies to improve ricinoleic acid yields, MudPIT analysis on endoplasmic reticulum (ER) purified from developing castor bean endosperm was performed and candidate enzymes for all steps of triacylglycerol synthesis were identified.
Journal ArticleDOI

Crystallization and preliminary X-ray analysis of the glycerol-3-phosphate 1-acyltransferase from squash (Cucurbita moschata).

TL;DR: Crystals of squash G3PAT have been obtained by the hanging-drop method of vapour diffusion using PEG 4000 as the precipitant, with approximate unit-cell parameters most likely to belong to space group P2(1)2( 1)2 (1) 2(1), and X-ray diffraction data to 1.3.9 A resolution have been collected in-house using a MAR 345 imaging-plate system.
Journal ArticleDOI

Inhibition and covalent modification of rape seed (Brassica napus) enoyl ACP reductase by phenylglyoxal

TL;DR: Results are consistent with there being two arginine residues either at the active site of the enzyme or in an environment which is protected from phenylglyoxal by a conformational change induced by coenzyme A binding.