ArticleThe Journal of biological chemistry2008
Methanogen homoaconitase catalyzes both hydrolyase reactions in coenzyme B biosynthesis.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 40 citations in OpenAlex.
- Fusion/fission protein family identification in Archaea.mSystems · 2024Article
- On the Evolutionary History of the Twenty Encoded Amino Acids.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Review
- Bovine host genome acts on rumen microbiome function linked to methane emissions.Communications biology · 2022Article
- Crystal structures of aconitase X enzymes from bacteria and archaea provide insights into the molecular evolution of the aconitase superfamily.Communications biology · 2021Article
- Methanogenesis on Early Stages of Life: Ancient but Not Primordial.Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life · 2018Article
- Functional characterization of aconitase X as a cis-3-hydroxy-L-proline dehydratase.Scientific reports · 2016Article
- Algorithmic co-optimization of genetic constructs and growth conditions: application to 6-ACA, a potential nylon-6 precursor.Nucleic acids research · 2015Article
- The fungal α-aminoadipate pathway for lysine biosynthesis requires two enzymes of the aconitase family for the isomerization of homocitrate to homoisocitrate.Molecular microbiology · 2012Article
- Antifungal activity of homoaconitate and homoisocitrate analogs.Molecules (Basel, Switzerland) · 2012Article
- Engineering synthetic recursive pathways to generate non-natural small molecules.Nature chemical biology · 2012Review
- More than 200 genes required for methane formation from H₂ and CO₂ and energy conservation are present in Methanothermobacter marburgensis and Methanothermobacter thermautotrophicus.Archaea (Vancouver, B.C.) · 2011Article
- Archaeal ApbC/Nbp35 homologs function as iron-sulfur cluster carrier proteins.Journal of bacteriology · 2009Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Homoaconitase enzymes catalyze hydrolyase reactions in the alpha-aminoadipate pathway for lysine biosynthesis or the 2-oxosuberate pathway for methanogenic coenzyme B biosynthesis. Despite the homology of this iron-sulfur protein to aconitase, previously studied homoaconitases catalyze only the hydration of cis-homoaconitate to form homoisocitrate rather than the complete isomerization of homocitrate to homoisocitrate. The MJ1003 and MJ1271 proteins from the methanogen Methanocaldococcus jannaschii formed the first homoaconitase shown to catalyze both the dehydration of (R)-homocitrate to form cis-homoaconitate, and its hydration is shown to produce homoisocitrate. This heterotetrameric enzyme also used the analogous longer chain substrates cis-(homo)(2)aconitate, cis-(homo)(3)aconitate, and cis-(homo)(4)aconitate, all with similar specificities. A combination of the homoaconitase with the M. jannaschii homoisocitrate dehydrogenase catalyzed all of the isomerization and oxidative decarboxylation reactions required to form 2-oxoadipate, 2-oxopimelate, and 2-oxosuberate, completing three iterations of the 2-oxoacid elongation pathway. Methanogenic archaeal homoaconitases and fungal homoaconitases evolved in parallel in the aconitase superfamily. The archaeal homoaconitases share a common ancestor with isopropylmalate isomerases, and both enzymes catalyzed the hydration of the minimal substrate maleate to form d-malate. The variation in substrate specificity among these enzymes correlated with the amino acid sequences of a flexible loop in the small subunits.
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