How enzyme promiscuity and horizontal gene transfer contribute to metabolic innovation

ME Glasner, DP Truong, BC Morse - The FEBS journal, 2020 - Wiley Online Library
Promiscuity is the coincidental ability of an enzyme to catalyze its native reaction and
additional reactions that are not biological functions in the same active site. Promiscuity …

Recent advances in enzyme promiscuity

RD Gupta - Sustainable Chemical Processes, 2016 - Springer
Enzyme promiscuity is defined as the capability of an enzyme to catalyze a reaction other
than the reaction for which it has been specialized. Although, enzyme is known for its …

Light-emitting dehalogenases: reconstruction of multifunctional biocatalysts

R Chaloupkova, V Liskova, M Toul, K Markova… - ACS …, 2019 - ACS Publications
To obtain structural insights into the emergence of biological functions from catalytically
promiscuous enzymes, we reconstructed an ancestor of catalytically distinct, but …

Complex Loop Dynamics Underpin Activity, Specificity, and Evolvability in the (βα)8 Barrel Enzymes of Histidine and Tryptophan Biosynthesis

A Romero-Rivera, M Corbella, A Parracino, WM Patrick… - JACS Au, 2022 - ACS Publications
Enzymes are conformationally dynamic, and their dynamical properties play an important
role in regulating their specificity and evolvability. In this context, substantial attention has …

Taking advantage of promiscuity of cold-active enzymes

SK Nandanwar, SB Borkar, JH Lee, HJ Kim - Applied Sciences, 2020 - mdpi.com
Cold-active enzymes increase their catalytic efficiency at low-temperature, introducing
structural flexibility at or near the active sites. Inevitably, this feat seems to be accompanied …

Evolution of substrate specificity in a retained enzyme driven by gene loss

AL Juarez-Vazquez, JN Edirisinghe… - Elife, 2017 - elifesciences.org
The connection between gene loss and the functional adaptation of retained proteins is still
poorly understood. We apply phylogenomics and metabolic modeling to detect bacterial …

Long-term persistence of bi-functionality contributes to the robustness of microbial life through exaptation

MG Plach, B Reisinger, R Sterner, R Merkl - PLoS genetics, 2016 - journals.plos.org
Modern enzymes are highly optimized biocatalysts that process their substrates with
extreme efficiency. Many enzymes catalyze more than one reaction; however, the …

[HTML][HTML] Interaction of antitubercular drug candidates with α1-acid glycoprotein produced in pulmonary granulomas

F Zsila, S Bősze, T Beke-Somfai - International journal of biological …, 2020 - Elsevier
The intracellular pathogen Mycobacterium tuberculosis can survive and replicate within host
macrophages. Among various immunomodulatory substances, macrophages also produce …

Two-step Ligand Binding in a (βα) 8 barrel enzyme: substrate-bound structures shed new light on the catalytic cycle of HisA

A Söderholm, X Guo, MS Newton, GB Evans… - Journal of Biological …, 2015 - ASBMB
HisA is a (βα) 8 barrel enzyme that catalyzes the Amadori rearrangement of N′-[(5′-
phosphoribosyl) formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (ProFAR) to …

Increasing metagenomic resolution of microbiome interactions through functional phylogenomics and bacterial sub-communities

A Cibrián-Jaramillo, F Barona-Gómez - Frontiers in Genetics, 2016 - frontiersin.org
The genomic composition of the microbiome and its relationship with the environment is an
exciting open question in biology. Metagenomics is a useful tool in the discovery of …