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Literature summary for 1.14.19.31 extracted from

  • Meyer, A.; Cirpus, P.; Ott, C.; Schlecker, R.; Zähringer, U.; Heinz, E.
    Biosynthesis of docosahexaenoic acid in Euglena gracilis: Biochemical and molecular evidence for the involvement of a DELTA4-fatty acyl group desaturase (2003), Biochemistry, 42, 9779-9788.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis Euglena gracilis
DNA and amino acid sequence determination and analysis Thraustochytrium sp.

Organism

Organism UniProt Comment Textmining
Euglena gracilis
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no activity in Crypthecodinium cohnii
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no activity in Schizochytrium sp.
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Thraustochytrium sp.
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme catalyzes the conversion of 2-docosapentaenoic acid (DPA, 22:5 DELTA7,10,13,16,19) to docosahexaenoic acid (DHA) by direct DELTA4-desaturation, not substrate breakdown and resynthesis. The enzyme shows strict DELTA4-regioselectivity and requires the presence of a DELTA7-double bond in the substrate. Positional analysis of phosphatidylcholine revealed that the proportion of the DELTA4-desaturated products is up to 20times higher in the sn-2 position than in the sn-1 position Euglena gracilis ?
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 ?
additional information the enzyme catalyzes the conversion of [2-(14)C]-docosapentaenoic acid (DPA, 22:5 DELTA7,10,13,16,19) to docosahexaenoic acid (DHA) by direct DELTA4-desaturation, not substrate breakdown and resynthesis. The enzyme shows strict DELTA4-regioselectivity and requires the presence of a DELTA7-double bond in the substrate. Positional analysis of phosphatidylcholine revealed that the proportion of the DELTA4-desaturated products is up to 20times higher in the sn-2 position than in the sn-1 position Thraustochytrium sp. ?
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 ?

Synonyms

Synonyms Comment Organism
DELTA4-fatty acid desaturase
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 Euglena gracilis
DELTA4-fatty acid desaturase
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 Thraustochytrium sp.