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Literature summary for 1.14.19.26 extracted from

  • Cahoon, E.B.; Lindqvist, Y.; Schneider, G.; Shanklin, J.
    Redesign of soluble fatty acid desaturases from plants from altered substrate specificity and double bond position (1997), Proc. Natl. Acad. Sci. USA, 94, 4872-4877.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.19.26

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli Thunbergia alata

Protein Variants

Protein Variants Comment Organism
A181T/A188G/Y189F/S205N/L206T/G207A the mutation yields an enzyme that functions primarily as a DELTA9-18:0-[acyl-carrier protein] desaturase. This enzyme displays only DELTA9 desaturase activity with 18:0-[acyl-carrier protein] and is nearly 4-fold more active with this substrate than with 16:0-[acyl-carrier protein]. Like mutant A181TyA200F, this enzyme retains DELTA6 desaturase activity with 16:0-[acyl-carrier protein] Thunbergia alata
A181T/A200F the mutation gives rise to an enzyme that catalyzed primarily the DELTA9 desaturation of 18:0-[acyl-carrier protein], but functions as a DELTA6 desaturase with 16:0-[acyl-carrier protein] Thunbergia alata
A181T/A200F/S205N/L206T/G207A replacement of specific amino acid residues in a DELTA6-palmitoyl (16:0)-[acyl-carrier protein] desaturase with their equivalents from a DELTA9-stearoyl (18:0)-[acyl-carrier protein] desaturase. The A181T/A200F/S205N/L206T/G207A mutant enzyme is functions principally as a DELTA9-18:0-[acyl-carrier protein] desaturase Thunbergia alata
A188G/Y189F mutant with broadened fatty acid chain-length specificity Thunbergia alata
additional information replacement of specific amino acid residues in a DELTA6-palmitoyl (16:0)-[acyl-carrier protein] desaturase with their equivalents from a DELTA9-stearoyl (18:0)-[acyl-carrier protein] desaturase, mutant enzymes are identified that have altered fatty acid chain-length specificities or that can insert double bonds into either the DELTA6 or DELTA9 positions of 16:0- and 18:0-[acyl-carrier protein] Thunbergia alata

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 palmitoyl-[acyl-carrier protein] Km-values determined for the wild-type enzyme and mutant A188G/Y189F are in the range of 0.2 to 0.6 mM with both 16:0- and 18:0-[acyl-carrier protein], suggesting that, at least in the case of these enzymes, changes in the substrate binding properties can be discounted as an underlying cause of differences in activities Thunbergia alata

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
palmitoyl-[acyl-carrier protein] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ Thunbergia alata
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 (Z)-hexadec-6-enoyl-[acyl-carrier protein] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Thunbergia alata Q41510
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-

Purification (Commentary)

Purification (Comment) Organism
-
 Thunbergia alata

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
palmitoyl-[acyl-carrier protein] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
-
 Thunbergia alata (Z)-hexadec-6-enoyl-[acyl-carrier protein] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
 ?

Synonyms

Synonyms Comment Organism
DELTA6-16:0-ACP desaturase
-
 Thunbergia alata
DELTA6-palmitoyl (16:0)-ACP desaturase
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 Thunbergia alata