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Literature summary for 4.2.1.96 extracted from

  • Pribat, A.; Noiriel, A.; Morse, A.M.; Davis, J.M.; Fouquet, R.; Loizeau, K.; Ravanel, S.; Frank, W.; Haas, R.; Reski, R.; Bedair, M.; Sumner, L.W.; Hanson, A.D.
    Nonflowering plants possess a unique folate-dependent phenylalanine hydroxylase that is localized in chloroplasts (2010), Plant Cell, 22, 3410-3422.
    View publication on PubMed
Search for more literature for 4.2.1.96

Cloned(Commentary)

Cloned (Comment) Organism
targeting of full-length GFP-tagged PCD sequence to chloroplasts in Arabidopsis thaliana mesophyll protoplasts Physcomitrium patens
targeting of full-length GFP-tagged PCD sequence to chloroplasts in Arabidopsis thaliana mesophyll protoplasts Pinus taeda

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast co-localization and complex formation with aromatic amino acid hydroxylase, AAH, overview Physcomitrium patens 9507
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chloroplast co-localization and complex formation with aromatic amino acid hydroxylase, AAH, overview Pinus taeda 9507
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Organism

Organism UniProt Comment Textmining
Physcomitrium patens
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-
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Pinus taeda
-
-
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Synonyms

Synonyms Comment Organism
PCD
-
 Physcomitrium patens
PCD
-
 Pinus taeda
Pterin-4a-carbinolamine dehydratase
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 Physcomitrium patens
Pterin-4a-carbinolamine dehydratase
-
 Pinus taeda

General Information

General Information Comment Organism
physiological function pterin-4a-carbinolamine dehydratase regenerates the tetrahydropterin-dependent aromatic amino acid hydroxylase, AAH, tetrahydropterin cofactor from 4a-carbinolamine Physcomitrium patens
physiological function pterin-4a-carbinolamine dehydratase regenerates the tetrahydropterin-dependent aromatic amino acid hydroxylase, AAH, tetrahydropterin cofactor from 4a-carbinolamine Pinus taeda