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Literature summary for 1.14.18.7 extracted from

  • Nagano, M.; Ihara-Ohori, Y.; Imai, H.; Inada, N.; Fujimoto, M.; Tsutsumi, N.; Uchimiya, H.; Kawai-Yamada, M.
    Functional association of cell death suppressor, Arabidopsis Bax inhibitor-1, with fatty acid 2-hydroxylation through cytochrome b5 (2009), Plant J., 58, 122-134.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
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Saccharomyces cerevisiae
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Synonyms

Synonyms Comment Organism
FAH1
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Saccharomyces cerevisiae
FAH1
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Arabidopsis thaliana
FAH2
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Arabidopsis thaliana

Cofactor

Cofactor Comment Organism Structure
cytochrome b5 Arabidopsis thaliana FAH1 and FAH2 have no Cb5-like domain, and interact with electron transfer protein Cb5. Bax inhibitor-1 is a widely conserved cytoprotective protein localized in the endoplasmic reticulum membrane and also interacts with Cb5. Arabidopsis thaliana Bax inhibitor-1 -mediated suppression of cell death in yeast requires Saccharomyces cerevisiae fatty acid hydroxylase 1, which has a Cb5-like domain at the N terminus and interacts with Bax inhibitor-1 Arabidopsis thaliana
cytochrome b5 fatty acid hydroxylase 1 has a Cb5-like domain at the N terminus and interacts with plant cryoprotective protein Bax inhibitor-1 Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function Arabidopsis thaliana Bax inhibitor-1 -mediated suppression of cell death in yeast requires Saccharomyces cerevisiae fatty acid hydroxylase 1, which has a Cb5-like domain at the N terminus and interacts with Bax inhibitor-1 Saccharomyces cerevisiae