5TMA

Zymomonas mobilis pyruvate decarboxylase mutant PDC-2.3

Summary for 5TMA

• Entry DOI: 10.2210/pdb5tma/pdb
• Descriptor: Pyruvate decarboxylase, THIAMINE DIPHOSPHATE, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: pyruvate decarboxylase, pdc, mutant, engineered, thermostable, cell adhesion
• Biological source: Zymomonas mobilis
• Total number of polymer chains: 2
• Total formula weight: 128430.74

Authors

Alahuhta, P.M.,Lunin, V.V. (deposition date: 2016-10-12, release date: 2017-10-18, Last modification date: 2023-10-04)

Primary citation

Sammond, D.W.,Kastelowitz, N.,Donohoe, B.S.,Alahuhta, M.,Lunin, V.V.,Chung, D.,Sarai, N.S.,Yin, H.,Mittal, A.,Himmel, M.E.,Guss, A.M.,Bomble, Y.J.
An iterative computational design approach to increase the thermal endurance of a mesophilic enzyme.
Biotechnol Biofuels, 11:189-189, 2018

PubMed Abstract: Strategies for maximizing the microbial production of bio-based chemicals and fuels include eliminating branched points to streamline metabolic pathways. While this is often achieved by removing key enzymes, the introduction of nonnative enzymes can provide metabolic shortcuts, bypassing branched points to decrease the production of undesired side-products. Pyruvate decarboxylase (PDC) can provide such a shortcut in industrially promising thermophilic organisms; yet to date, this enzyme has not been found in any thermophilic organism. Incorporating nonnative enzymes into host organisms can be challenging in cases such as this, where the enzyme has evolved in a very different environment from that of the host.

PubMed: 30002729
DOI: 10.1186/s13068-018-1178-9

Experimental method

X-RAY DIFFRACTION (1.67 Å)