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

. 2021 Jan 11;11:277. doi: 10.1038/s41598-020-79489-3

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

© The Author(s) 2021

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Structural insights into the catalytic mechanism of Tl-Cyn. (a) Schematic drawing of the detailed interactions between Tl-Cyn and the malonate molecule bound in the active site (sticks model and labeled Mal). Hydrogen-bonding interactions with the malonate are indicated with dashed lines (red). (b) Close-up view to that in (a), and the internal cavity for malonate is shown with semi-transparent surface. (c) Conserved sequence near the active site region of the C-terminal domain in fungal cyanases are shown in cyan. Residues that interact with Mal are shown with yellow background. Tl: Thermomyces lanuginosus, Af: Aspergillus flavus, Ps: Penicillium subrubescens, Pc: Phaeomoniella chlamydospora, Fp: Fonsecaea pedrosoi, Rm: Rhinocladiella mackenziei. (d) Catalytic activities of wild-type (WT) and mutant Tl-Cyn. The cyanate concentration is at 2 mM. The error bars represent the standard deviation from three independent measurements. NA, no activity observed under the condition tested. (e) Sequence alignment for the N-terminal domain of the fungal cyanases. Conserved residues are in cyan and a unique Y14 residue in Tl-Cyn is shown with yellow background.