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Literature summary extracted from

  • Lakhssassi, N.; Colantonio, V.; Flowers, N.D.; Zhou, Z.; Henry, J.; Liu, S.; Meksem, K.
    Stearoyl-acyl carrier protein desaturase mutations uncover an impact of stearic acid in leaf and nodule structure (2017), Plant Physiol., 174, 1531-1543 .
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
1.14.19.2 biotechnology random mutagenesis and mutational analysis allows for the achievement of high seed stearic acid content with no associated negative agronomic characteristics, raandom mutagenesis as a rheostat for agronomically important traits Glycine max

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.19.2 gene Gmsacpd-c, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time PCR enzyme expression analysis Glycine max

Protein Variants

EC Number Protein Variants Comment Organism
1.14.19.2 C235T random mutagenesis Glycine max
1.14.19.2 C247T random mutagenesis Glycine max
1.14.19.2 C305T random mutagenesis Glycine max
1.14.19.2 D77N random mutagenesis, the alteration of charge in the missense mutants SACPD-CD77N is due to the iron ion pocket localization, the mutation is predicted to affect iron ion-binding kinetics and stability Glycine max
1.14.19.2 E114K random mutagenesis, the mutation directly alters the negatively charged bridging ligand Glu114 into a positively charged Lys Glycine max
1.14.19.2 G1777A random mutagenesis Glycine max
1.14.19.2 G1964T random mutagenesis Glycine max
1.14.19.2 G229A random mutagenesis Glycine max
1.14.19.2 G340A random mutagenesis Glycine max
1.14.19.2 L79F random mutagenesis, the alteration of charge in the missense mutants SACPD-CD77N is due to the iron ion pocket localization, presence of steric hindrance by L79F, the mutation is predicted to affect iron ion-binding kinetics and stability Glycine max
1.14.19.2 additional information one nonsense and four missense Gmsacpd-c mutants are identified to have high levels of seed, nodule, and leaf stearic acid content. Homology modeling and in silico analysis of the GmSACPD-C enzyme reveals that most of these mutations are localized near or at conserved residues essential for di-iron ion coordination. Soybeans carrying Gmsacpd-c mutations at conserved residues show the highest stearic acid content, and these mutations have deleterious effects on nodule development and function. Nodule leghemoglobin transcripts are significantly more abundant in soybeans with deleterious mutations at conserved residues of GmSACPD-C. Gmsacpd-c mutations cause an increase in leaf stearic acid content and an alteration of leaf structure and morphology in addition to differences in nitrogen-fixing nodule structure. Wild-type and mutant leaf phenotypes, overview Glycine max
1.14.19.2 P102L random mutagenesis, the missense mutant SACPD-CP102L is not localized at the iron ion-binding pocket but is positioned at the first residue of the alpha4 chain,which holds the ligands Glu114 and His117 in place. Considering Pro's cyclic conformation, in which the secondary amine binds to the alha-carbon of the protein backbone, a disruption of this conformational rigidity may impact the ability of the alpha4 chain to be in its proper location, disrupting the enzymatic activity of GmSACPD-C Glycine max

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.19.2 Fe2+ ferredoxin [iron-sulfur] cluster Glycine max

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.19.2 stearoyl-[acyl-carrier protein] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ Glycine max
-
 oleoyl-[acyl-carrier protein] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.19.2 Glycine max
-
 cv. Forrest
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.19.2 leaf wild-type and mutant leaf phenotypes, overview Glycine max
-
1.14.19.2 root nodule
-
 Glycine max
-
1.14.19.2 seed
-
 Glycine max
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.19.2 stearoyl-[acyl-carrier protein] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+
-
 Glycine max oleoyl-[acyl-carrier protein] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.19.2 Gmsacpd-c
-
 Glycine max
1.14.19.2 SACPD
-
 Glycine max
1.14.19.2 SACPD-C
-
 Glycine max
1.14.19.2 SAD
-
 Glycine max
1.14.19.2 stearoyl-acyl carrier protein desaturase
-
 Glycine max

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.19.2 Ferredoxin
-
 Glycine max

General Information

EC Number General Information Comment Organism
1.14.19.2 malfunction one nonsense and four missense Gmsacpd-c mutants are identified to have high levels of seed, nodule, and leaf stearic acid content. Homology modeling and in silico analysis of the GmSACPD-C enzyme reveals that most of these mutations are localized near or at conserved residues essential for di-iron ion coordination. Soybeans carrying Gmsacpd-c mutations at conserved residues cause the highest stearic acid content, and these mutations have deleterious effects on nodule development and function. Mutant plants with mutations at nonconserved residues show an increase in stearic acid content yet retain healthy nodules. Nodule leg hemoglobin transcripts are significantly more abundant in soybeans with deleterious mutations at conserved residues of GmSACPD-C. Gmsacpd-c mutations cause an increase in leaf stearic acid content and an alteration of leaf structure and morphology in addition to differences in nitrogen-fixing nodule structure. Wild-type and mutant leaf phenotypes, overview Glycine max
1.14.19.2 additional information homology modeling of GmSACPD-C from cv. Forrest with important catalytic residues and the five identified sacpd-c missense mutations mapped, overview Glycine max