Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2020 Feb 10;10:2292. doi: 10.1038/s41598-020-59120-1

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Dependence of rFAAH activity on substrate concentration. (a) Dependence of rFAAH activity on substrate concentration, interpolated through the Hill equation; (b) rFAAH shows a canonical sigmoidal curve in the presence of increasing concentration of the AAMCA substrate, that is not fitted equally well by non-linear regression through the Michaelis-Menten equation; (c) rFAAH in the presence of URB597 at a homodimer:inhibitor 1:0.5 molar ratio shows a sigmoidal behaviour; (d) Kinetic analysis of rFAAH F432A mutant indicates that P432 residue is involved in the catalytic activity of the enzyme, but not in the modulation of cooperativity; (e) Kinetic analysis of rFAAH W445Y mutant interpolated through the Hill formalism; (f) Kinetic analysis of rFAAH W445Y mutant shows loss of the sigmoidal behaviour, leading to a canonical hyperbolic Michaelis-Menten enzyme without any cooperativity.