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Understanding the molecular properties of the E1 subunit (SucA) of alpha-ketoglutarate dehydrogenase complex from Vibrio vulnificus for the enantioselective ligation of acetaldehydes into (R)-acetoin

Title
Understanding the molecular properties of the E1 subunit (SucA) of alpha-ketoglutarate dehydrogenase complex from Vibrio vulnificus for the enantioselective ligation of acetaldehydes into (R)-acetoin
Authors
Seo, Pil-WonJo, Hye-JinHwang, In YeubJeong, Ha-YeonKim, Jun-HongKim, Ji-WonLee, Eun YeolPark, Jin-ByungKim, Jeong-Sun
Ewha Authors
박진병
SCOPUS Author ID
박진병scopus
Issue Date
2020
Journal Title
CATALYSIS SCIENCE & TECHNOLOGY
ISSN
2044-4753JCR Link

2044-4761JCR Link
Citation
CATALYSIS SCIENCE & TECHNOLOGY vol. 10, no. 1, pp. 79 - 85
Publisher
ROYAL SOC CHEMISTRY
Indexed
SCIE; SCOPUS WOS scopus
Document Type
Article
Abstract
Escherichia coli SucA, a decarboxylating E1 component of the a-ketoglutarate dehydrogenase complex, has been reported to possess another catalytic activity in carboligating two acetaldehyde molecules to form acetoin in a thiamine diphosphate (ThDP)-dependent manner. Here, we examined acetoin formation activity from acetaldehyde using SucAs from various organisms, as well as the Zymomonas pyruvate decarboxylase (ZmPDC) and the formaldehyde-ligating formolase. Among the studied SucA enzymes, Vibrio vulnificus SucA (VvSucA) exhibited the highest ligating activity against acetaldehyde with an excellent enantioselectivity of the product in contrast to ZmPDC and formolase of poor enantioselectivity. The revealed VvSucA structure shows a dimeric assembly with the bound ThDP within the active sites at the two-subunit interface. Non-covalently bound glycolaldehyde molecules suggest the two substrate-binding sites within the carboligating active site for acetaldehyde. Structure-guided mutants reveal residues critical for regiospecificity of VvSucA. The obtained biochemical and structural data help to understand the high enantioselective ligation of two acetaldehyde molecules by VvSucA.
DOI
10.1039/c9cy01566c
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엘텍공과대학 > 식품공학전공 > Journal papers
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