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Literature summary for 1.14.19.33 extracted from

  • Rawat, R.; Yu, X.H.; Sweet, M.; Shanklin, J.
    Conjugated fatty acid synthesis: residues 111 and 115 influence product partitioning of Momordica charantia conjugase (2012), J. Biol. Chem., 287, 16230-16237.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene FADX, sequence comparisons, recombinant expression of enzyme mutant chimeras in the Arabidopsis thaliana fad3fae1 mutant strain, lacks the activity of both the endoplasmic reticulum omega-3 desaturase (FAD3) and the fatty acid elongation 1 (FAE1)-condensing enzyme, as well as elevated levels of linoleic acid Momordica charantia

Protein Variants

Protein Variants Comment Organism
D115E site-directed mutagenesis, the mutant shows reaction product like the wild-type enzyme, predominantly alpha-eleostearic acid and little punicic acid Momordica charantia
G111V site-directed mutagenesis, the mutant shows reaction product like the wild-type enzyme, predominantly alpha-eleostearic acid and little punicic acid Momordica charantia
G111V/D115E site-directed mutagenesis, the mutant shows reaction product unlike the wild-type enzyme, approximately equal amounts of alpha-eleostearic acidandits isomer, punicic acid Momordica charantia
additional information construction of a series of Momordica charantia FADX-Arabidopsis thaliana FAD2 chimeras: chimera 1 contains Momordica FADX amino acids 1-157 and Arabidopsis FAD2 amino acids 149-383, chimera 2 contains FADX aa 1–210 with FAD2 aa 202-383, chimera 3 contains FADX aa 1-252 with FAD2 aa 244-383, chimera 4 contains FADX aa 1-326 with FAD2 aa 317-383, chimera 5 contains FAD2 aa 1-52 with FADX aa 61-399, chimera 6 contains FAD2 aa 1-83 with FADX aa 93-399, chimera 7 contains FAD2 aa 1-116 with FADX aa 126-399, and chimera 8 containsFAD2 aa 1-148 with FADX aa 158-399, mutant product formations, overview. Analysis of a FADX mutant containing six substitutions in which the sequence of helix 2 and first histidine box is converted to that of FAD2 Momordica charantia

Organism

Organism UniProt Comment Textmining
Momordica charantia Q9SP61 gene FADX
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the wild-type enzyme produces predominantly conjugated alpha-eleostearic acid and little punicic acid from its substrate linoleic acid. The helix 2 and the first histidine box are a determinant of conjugase product partitioning into alpha-punicic acid ((9Z,11E,13E,15Z)-octadeca-9,11,13,15-tetraenoate) or alpha-eleostearic acid ((9Z,11E,13E)-octadeca-9,11,13-trienoate), sequence comparisons, overview. Residues 111 and 115 of the enzyme exhibit an interactive effect in punicic acid formation Momordica charantia ?
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Synonyms

Synonyms Comment Organism
FADX
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Momordica charantia