Structural insight into bi-functional malonyl-CoA reductase.

Szczegóły
Abstrakt

Tytuł:: Structural insight into bi-functional malonyl-CoA reductase.
Autorzy:: Son HF; School of Life Sciences (KNU Creative BioResearch Group), KNU Institute for Microorganisms, Kyungpook National University, Daegu, South Korea.
Kim S; School of Life Sciences (KNU Creative BioResearch Group), KNU Institute for Microorganisms, Kyungpook National University, Daegu, South Korea.
Seo H; School of Life Sciences (KNU Creative BioResearch Group), KNU Institute for Microorganisms, Kyungpook National University, Daegu, South Korea.
Hong J; School of Life Sciences (KNU Creative BioResearch Group), KNU Institute for Microorganisms, Kyungpook National University, Daegu, South Korea.
Lee D; School of Life Sciences (KNU Creative BioResearch Group), KNU Institute for Microorganisms, Kyungpook National University, Daegu, South Korea.
Jin KS; Pohang Accelerator Laboratory, Pohang University of Science and Technology, Pohang, South Korea.
Park S; School of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST), Ulsan, South Korea.
Kim KJ; School of Life Sciences (KNU Creative BioResearch Group), KNU Institute for Microorganisms, Kyungpook National University, Daegu, South Korea.
Źródło:: Environmental microbiology [Environ Microbiol] 2020 Feb; Vol. 22 (2), pp. 752-765. Date of Electronic Publication: 2019 Dec 20.
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
Język:: English
Imprint Name(s):: Original Publication: Oxford : Blackwell Science, 1999-
MeSH Terms:: Alphaproteobacteria/*enzymology
Malondialdehyde/*analogs & derivatives
Malonyl Coenzyme A/*metabolism
Oxidoreductases/*metabolism
Binding Sites/physiology ; Lactic Acid/analogs & derivatives ; Lactic Acid/metabolism ; Malondialdehyde/metabolism ; Phylogeny ; Protein Binding/physiology ; Protein Conformation
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Grant Information:: NRF-2018H1A2A1061751 International NRF-2018-Global PhD Fellowship Program of the Korean Government; NRF-2016M3D3A1A01913269 International Ministry of Science and ICT; International National Research Foundation of Korea
Substance Nomenclature:: 33X04XA5AT (Lactic Acid)
4Y8F71G49Q (Malondialdehyde)
524-14-1 (Malonyl Coenzyme A)
9K1T0U0R4C (malonic semialdehyde)
C4ZF6XLD2X (hydracrylic acid)
EC 1.- (Oxidoreductases)
EC 1.- (malonyl-Coa reductase)
SCR Organism:: Porphyrobacter dokdonensis
Entry Date(s):: Date Created: 20191210 Date Completed: 20200907 Latest Revision: 20200907
Update Code:: 20240105
DOI:: 10.1111/1462-2920.14885
PMID:: 31814251
: Czasopismo naukowe

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The bi-functional malonyl-CoA reductase is a key enzyme of the 3-hydroxypropionate bi-cycle for bacterial CO 2 fixation, catalysing the reduction of malonyl-CoA to malonate semialdehyde and further reduction to 3-hydroxypropionate. Here, we report the crystal structure and the full-length architecture of malonyl-CoA reductase from Porphyrobacter dokdonensis. The malonyl-CoA reductase monomer of 1230 amino acids consists of four tandemly arranged short-chain dehydrogenases/reductases, with two catalytic and two non-catalytic short-chain dehydrogenases/reductases, and forms a homodimer through paring contact of two malonyl-CoA reductase monomers. The complex structures with its cofactors and substrates revealed that the malonyl-CoA substrate site is formed by the cooperation of two short-chain dehydrogenases/reductases and one novel extra domain, while only one catalytic short-chain dehydrogenase/reductase contributes to the formation of the malonic semialdehyde-binding site. The phylogenetic and structural analyses also suggest that the bacterial bi-functional malonyl-CoA has a structural origin that is completely different from the archaeal mono-functional malonyl-CoA and malonic semialdehyde reductase, and thereby constitute an efficient enzyme.
(© 2019 Society for Applied Microbiology and John Wiley & Sons Ltd.)

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