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Structural insights into bifunctional thaumarchaeal crotonyl-CoA hydratase and 3-hydroxypropionyl-CoA dehydratase from Nitrosopumilus maritimus
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Structural insights into bifunctional thaumarchaeal crotonyl-CoA hydratase and 3-hydroxypropionyl-CoA dehydratase from Nitrosopumilus maritimus
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Journal Article
Structural insights into bifunctional thaumarchaeal crotonyl-CoA hydratase and 3-hydroxypropionyl-CoA dehydratase from Nitrosopumilus maritimus
2021
Overview
The ammonia-oxidizing thaumarchaeal 3-hydroxypropionate/4-hydroxybutyrate (3HP/4HB) cycle is one of the most energy-efficient CO
2
fixation cycles discovered thus far. The protein encoded by Nmar_1308 (from
Nitrosopumilus maritimus
SCM1) is a promiscuous enzyme that catalyzes two essential reactions within the thaumarchaeal 3HP/4HB cycle, functioning as both a crotonyl-CoA hydratase (CCAH) and 3-hydroxypropionyl-CoA dehydratase (3HPD). In performing both hydratase and dehydratase activities, Nmar_1308 reduces the total number of enzymes necessary for CO
2
fixation in Thaumarchaeota, reducing the overall cost for biosynthesis. Here, we present the first high-resolution crystal structure of this bifunctional enzyme with key catalytic residues in the thaumarchaeal 3HP/4HB pathway.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 631/61
/ Acyl Coenzyme A - metabolism
/ Ammonia
/ Archaeal Proteins - chemistry
/ Archaeal Proteins - genetics
/ Archaeal Proteins - metabolism
/ Enoyl-CoA Hydratase - chemistry
/ Enoyl-CoA Hydratase - genetics
/ Enoyl-CoA Hydratase - metabolism
/ Enzymes
/ Humanities and Social Sciences
/ Science
