Visualizing the Chain-Flipping Mechanism in Fatty-Acid Biosynthesis

The acyl carrier protein (ACP) from fatty acid synthases sequesters elongating products within its hydrophobic core, but this dynamic mechanism remains poorly understood. We exploited solvatochromic pantetheine probes attached to ACP that fluoresce when sequestered. The addition of a catalytic partn...

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Bibliographic Details
Published in:	Angewandte Chemie (International ed.) Vol. 53; no. 52; pp. 14456 - 14461
Main Authors:	Beld, Joris, Cang, Hu, Burkart, Michael D.
Format:	Journal Article
Language:	English
Published:	Weinheim WILEY-VCH Verlag 22.12.2014 WILEY‐VCH Verlag Wiley Wiley Subscription Services, Inc
Edition:	International ed. in English
Subjects:	acyl carrier protein Acyl Carrier Protein - chemistry Acyl Carrier Protein - metabolism BASIC BIOLOGICAL SCIENCES Biosynthesis Carriers Catalysis Catalysts chain-flipping mechanism Chains Chemistry Chemistry, Multidisciplinary E coli Elongation Escherichia coli fatty acid synthase Fatty acids Fatty Acids - biosynthesis Fluorescence Naphthalimides - chemistry Nuclear Magnetic Resonance, Biomolecular Oxadiazoles - chemistry Physical Sciences Protein Interaction Domains and Motifs Proteins Rhodamines - chemistry Science & Technology solvatochromism Solvents - chemistry DOMAIN fatty acids ESCHERICHIA-COLI chain-flipping mechanism SYNTHASE BETA-KETOACYL acyl carrier protein FLUORESCENCE SPECTROSCOPY fatty acid synthase SPINACH DYNAMICS solvatochromism
ISSN:	1433-7851, 1521-3773, 1521-3773
Online Access:	Get full text
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