6XEX

Structure of Serratia marcescens 2,3-butanediol dehydrogenase mutant Q247A/V139Q

Summary for 6XEX

• Entry DOI: 10.2210/pdb6xex/pdb
• Descriptor: 2,3-butanediol dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, SODIUM ION, ... (5 entities in total)
• Functional Keywords: bdh, oxidoreductase
• Biological source: Serratia marcescens
• Total number of polymer chains: 2
• Total formula weight: 56843.16

Authors

Alahuhta, P.M.,Lunin, V.V. (deposition date: 2020-06-14, release date: 2020-12-23, Last modification date: 2023-10-18)

Primary citation

Subramanian, V.,Lunin, V.V.,Farmer, S.J.,Alahuhta, M.,Moore, K.T.,Ho, A.,Chaudhari, Y.B.,Zhang, M.,Himmel, M.E.,Decker, S.R.
Phylogenetics-based identification and characterization of a superior 2,3-butanediol dehydrogenase for Zymomonas mobilis expression.
Biotechnol Biofuels, 13:186-186, 2020

PubMed Abstract: Zymomonas mobilis has recently been shown to be capable of producing the valuable platform biochemical, 2,3-butanediol (2,3-BDO). Despite this capability, the production of high titers of 2,3-BDO is restricted by several physiological parameters. One such bottleneck involves the conversion of acetoin to 2,3-BDO, a step catalyzed by 2,3-butanediol dehydrogenase (Bdh). Several Bdh enzymes have been successfully expressed in Z. mobilis, although a highly active enzyme is yet to be identified for expression in this host. Here, we report the application of a phylogenetic approach to identify and characterize a superior Bdh, followed by validation of its structural attributes using a mutagenesis approach.

PubMed: 33292448
DOI: 10.1186/s13068-020-01820-x

Experimental method

X-RAY DIFFRACTION (1.8 Å)