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Phylogeny and evolution of aldehyde dehydrogenase-homologous folate enzymes.

Publication ,  Journal Article
Strickland, KC; Holmes, RS; Oleinik, NV; Krupenko, NI; Krupenko, SA
Published in: Chem Biol Interact
May 30, 2011

Folate coenzymes function as one-carbon group carriers in intracellular metabolic pathways. Folate-dependent reactions are compartmentalized within the cell and are catalyzed by two distinct groups of enzymes, cytosolic and mitochondrial. Some folate enzymes are present in both compartments and are likely the products of gene duplications. A well-characterized cytosolic folate enzyme, FDH (10-formyltetrahydro-folate dehydrogenase, ALDH1L1), contains a domain with significant sequence similarity to aldehyde dehydrogenases. This domain enables FDH to catalyze the NADP(+)-dependent conversion of short-chain aldehydes to corresponding acids in vitro. The aldehyde dehydrogenase-like reaction is the final step in the overall FDH mechanism, by which a tetrahydrofolate-bound formyl group is oxidized to CO(2) in an NADP(+)-dependent fashion. We have recently cloned and characterized another folate enzyme containing an ALDH domain, a mitochondrial FDH. Here the biological roles of the two enzymes, a comparison of the respective genes, and some potential evolutionary implications are discussed. The phylogenic analysis suggests that the vertebrate ALDH1L2 gene arose from a duplication event of the ALDH1L1 gene prior to the emergence of osseous fish >500 millions years ago.

Duke Scholars

Published In

Chem Biol Interact

DOI

EISSN

1872-7786

Publication Date

May 30, 2011

Volume

191

Issue

1-3

Start / End Page

122 / 128

Location

Ireland

Related Subject Headings

  • Toxicology
  • Sequence Homology, Amino Acid
  • Phylogeny
  • Oxidoreductases Acting on CH-NH Group Donors
  • Invertebrates
  • Humans
  • Genomics
  • Folic Acid
  • Exons
  • Evolution, Molecular
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Strickland, K. C., Holmes, R. S., Oleinik, N. V., Krupenko, N. I., & Krupenko, S. A. (2011). Phylogeny and evolution of aldehyde dehydrogenase-homologous folate enzymes. Chem Biol Interact, 191(1–3), 122–128. https://doi.org/10.1016/j.cbi.2010.12.025
Strickland, Kyle C., Roger S. Holmes, Natalia V. Oleinik, Natalia I. Krupenko, and Sergey A. Krupenko. “Phylogeny and evolution of aldehyde dehydrogenase-homologous folate enzymes.Chem Biol Interact 191, no. 1–3 (May 30, 2011): 122–28. https://doi.org/10.1016/j.cbi.2010.12.025.
Strickland KC, Holmes RS, Oleinik NV, Krupenko NI, Krupenko SA. Phylogeny and evolution of aldehyde dehydrogenase-homologous folate enzymes. Chem Biol Interact. 2011 May 30;191(1–3):122–8.
Strickland, Kyle C., et al. “Phylogeny and evolution of aldehyde dehydrogenase-homologous folate enzymes.Chem Biol Interact, vol. 191, no. 1–3, May 2011, pp. 122–28. Pubmed, doi:10.1016/j.cbi.2010.12.025.
Strickland KC, Holmes RS, Oleinik NV, Krupenko NI, Krupenko SA. Phylogeny and evolution of aldehyde dehydrogenase-homologous folate enzymes. Chem Biol Interact. 2011 May 30;191(1–3):122–128.
Journal cover image

Published In

Chem Biol Interact

DOI

EISSN

1872-7786

Publication Date

May 30, 2011

Volume

191

Issue

1-3

Start / End Page

122 / 128

Location

Ireland

Related Subject Headings

  • Toxicology
  • Sequence Homology, Amino Acid
  • Phylogeny
  • Oxidoreductases Acting on CH-NH Group Donors
  • Invertebrates
  • Humans
  • Genomics
  • Folic Acid
  • Exons
  • Evolution, Molecular