ArticleProceedings of the National Academy of Sciences of the United States of America1999
Purification, molecular cloning, and expression of 2-hydroxyphytanoyl-CoA lyase, a peroxisomal thiamine pyrophosphate-dependent enzyme that catalyzes the carbon-carbon bond cleavage during alpha-oxidation of 3-methyl-branched fatty acids.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 114 citations in OpenAlex.
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- LRRC71 is essential for sperm motility, fertilization, and male fertility.The Journal of biological chemistry · 2026Article
- Revealing reaction intermediates in one-carbon elongation by thiamine diphosphate/CoA-dependent enzyme family.Communications chemistry · 2024Article
- The Weight of Bariatric Surgery: Wernicke-Korsakoff Syndrome after Vertical Sleeve Gastrectomy-A Case Series.Journal of personalized medicine · 2024Article
- Sodium Metabisulfite InhibitsPathogens (Basel, Switzerland) · 2024Article
- Transcriptome profiling reveals multiple regulatory pathways of Tamarix chinensis in response to salt stress.Plant cell reports · 2023Article
- The importance of thiamine (vitamin B1) in humans.Bioscience reports · 2023Article
- Role of 2-hydroxy acyl-CoA lyase HACL2 in odd-chain fatty acid production via α-oxidation in vivo.Molecular biology of the cell · 2023Article
- Synthetic Thioesters of Thiamine: Promising Tools for Slowing Progression of Neurodegenerative Diseases.International journal of molecular sciences · 2023Review
- A conserved oxalyl-coenzyme A decarboxylase in oxalate catabolism.Plant signaling & behavior · 2022Article
- Mitochondrial transport and metabolism of the vitamin B-derived cofactors thiamine pyrophosphate, coenzyme A, FAD and NADIUBMB life · 2022Review
- Comparative metabolomics with Metaboseek reveals functions of a conserved fat metabolism pathway in C. elegans.Nature communications · 2022Article
- Dysfunctional peroxisomal lipid metabolisms and their ocular manifestations.Frontiers in cell and developmental biology · 2022Review
- Transcriptome Profiling of the Salt Stress Response in the Leaves and Roots of HalophyticFrontiers in genetics · 2021Article
- Article
- 2-Hydroxy-Docosahexaenoic Acid Is Converted Into Heneicosapentaenoic Acid via α-Oxidation: Implications for Alzheimer's Disease Therapy.Frontiers in cell and developmental biology · 2020Article
- Actinobacterial Degradation of 2-Hydroxyisobutyric Acid Proceeds via Acetone and Formyl-CoA by Employing a Thiamine-Dependent Lyase Reaction.Frontiers in microbiology · 2020Article
- Peroxisomal Metabolite and Cofactor Transport in Humans.Frontiers in cell and developmental biology · 2020Review
- Functional analysis of the third identified SLC25A19 mutation causative for the thiamine metabolism dysfunction syndrome 4.Journal of human genetics · 2019Article
- 2-Hydroxyacyl-CoA lyase catalyzes acyloin condensation for one-carbon bioconversion.Nature chemical biology · 2019Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the third step of the alpha-oxidation of 3-methyl-branched fatty acids such as phytanic acid, a 2-hydroxy-3-methylacyl-CoA is cleaved into formyl-CoA and a 2-methyl-branched fatty aldehyde. The cleavage enzyme was purified from the matrix protein fraction of rat liver peroxisomes and identified as a protein made up of four identical subunits of 63 kDa. Its activity proved to depend on Mg(2+) and thiamine pyrophosphate, a hitherto unrecognized cofactor of alpha-oxidation. Formyl-CoA and 2-methylpentadecanal were identified as reaction products when the purified enzyme was incubated with 2-hydroxy-3-methylhexadecanoyl-CoA as the substrate. Hence the enzyme catalyzes a carbon-carbon cleavage, and we propose calling it 2-hydroxyphytanoyl-CoA lyase. Sequences derived from tryptic peptides of the purified rat protein were used as queries to recover human expressed sequence tags from the databases. The composite cDNA sequence of the human lyase contained an ORF of 1,734 bases that encodes a polypeptide with a calculated molecular mass of 63,732 Da. Recombinant human protein, expressed in mammalian cells, exhibited lyase activity. The lyase displayed homology to a putative Caenorhabditis elegans protein that resembles bacterial oxalyl-CoA decarboxylases. Similarly to the decarboxylases, a thiamine pyrophosphate-binding consensus domain was present in the C-terminal part of the lyase. Although no peroxisome targeting signal, neither 1 nor 2, was apparent, transfection experiments with constructs encoding green fluorescent protein fused to the full-length lyase or its C-terminal pentapeptide indicated that the C terminus of the lyase represents a peroxisome targeting signal 1 variant.
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