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 |
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 |
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 |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.14.19.2 | Fe2+ | ferredoxin [iron-sulfur] cluster | Glycine max |
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 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.19.2 | Glycine max | - |
cv. Forrest | - |
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 | - |
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 | - |
? |
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 |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.19.2 | Ferredoxin | - |
Glycine max |
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 |