Any feedback?
Literature summary extracted from
- Molecular mechanisms underlying catalytic activity of delta 6 desaturase from Glossomastix chrysoplasta and Thalassiosira pseudonana (2017), J. Lipid Res., 59, 79-88 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.14.19.3 | gene D6, recombinant expression in Saccharomyces | Glossomastix chrysoplasta |
| 1.14.19.3 | gene desI, recombinant expression in Saccharomyces | Thalassiosira pseudonana |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.14.19.3 | D313I | site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme | Glossomastix chrysoplasta |
| 1.14.19.3 | D367H | site-directed mutagenesis, mutant shows similar activity compared to the wild-type enzyme | Glossomastix chrysoplasta |
| 1.14.19.3 | F310L | site-directed mutagenesis, mutant shows similar activity compared to the wild-type enzyme | Glossomastix chrysoplasta |
| 1.14.19.3 | H360D | site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme | Thalassiosira pseudonana |
| 1.14.19.3 | H381N | site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme | Thalassiosira pseudonana |
| 1.14.19.3 | I306L | site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme | Thalassiosira pseudonana |
| 1.14.19.3 | I390L | site-directed mutagenesis, mutant shows similar activity with linoleoyl-CoA and reduced activity with alpha-linolenoyl-CoA compared to the wild-type enzyme | Glossomastix chrysoplasta |
| 1.14.19.3 | L303F | site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme | Thalassiosira pseudonana |
| 1.14.19.3 | L383I | site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme | Thalassiosira pseudonana |
| 1.14.19.3 | M384S/M385 | site-directed mutagenesis, mutant shows reduced activity compared to the wild-type enzyme | Thalassiosira pseudonana |
| 1.14.19.3 | M384S/M385L | site-directed mutagenesis, mutant shows significantly increased activity compared to the wild-type enzyme | Glossomastix chrysoplasta |
| 1.14.19.3 | additional information | construction of chimeric enzymes of delta6 desaturases from Glossomastix chrysoplasta and Thalassiosira pseudonana, chimera 7 with GcFADS2 residues 285-315 replaced by TpFADS2 residues 291-324 shows about 5fold increased activity with both substrates compared to the wild-type enzyme, the catalytic efficiency of chimera 9 with GcFADS2 residues 359-458 replaced by TpFADS2 residues 370-484 is also increased. The other chimeras exhibit a catalytic efficiency not significantly different both substrates compared with that exhibited by wild-type GcFADS2/TpFADS2. Fatty acid contents of wild-type and mutant strains, overview | Glossomastix chrysoplasta |
| 1.14.19.3 | additional information | construction of chimeric enzymes of delta6 desaturases from Glossomastix chrysoplasta and Thalassiosira pseudonana, e.g. chimera 16 with TpFADS2 residues 291-324 replaced by GcFADS2 residues 285-315 shows decreased activity with both substrates compared to the wild-type enzyme. The replacement of the aa359-458 region of GcFADS2 results in a significant reduction in catalytic activity against both substrates, such that chimera 18 exhibits a decreased catalytic efficiency which represents the lowest rate observed among the TpFADS2 chimeras. The other chimeras exhibit a catalytic efficiency not significantly different both substrates compared with that exhibited by wild-type GcFADS2/TpFADS2. Fatty acid contents of wild-type an dmutant strains, overview | Thalassiosira pseudonana |
| 1.14.19.3 | N388H | site-directed mutagenesis, mutant shows similar activity compared to the wild-type enzyme | Glossomastix chrysoplasta |
| 1.14.19.3 | S306T | site-directed mutagenesis, mutant shows similar activity compared to the wild-type enzyme | Glossomastix chrysoplasta |
| 1.14.19.3 | S322A | site-directed mutagenesis, mutant shows reduced activity compared to the wild-type enzyme | Thalassiosira pseudonana |
| 1.14.19.3 | S322A | site-directed mutagenesis, mutant shows highly increased activity compared to the wild-type enzyme | Glossomastix chrysoplasta |
| 1.14.19.3 | T299S | site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme | Thalassiosira pseudonana |
| 1.14.19.3 | T302V | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Thalassiosira pseudonana |
| 1.14.19.3 | T302V | site-directed mutagenesis, mutant shows highly increased activity compared to the wild-type enzyme | Glossomastix chrysoplasta |
| 1.14.19.3 | T302V | site-directed mutagenesis, mutant shows potently increased activity compared to the wild-type enzyme | Glossomastix chrysoplasta |
| 1.14.19.3 | Y375F | site-directed mutagenesis, mutant shows reduced activity compared to the wild-type enzyme | Thalassiosira pseudonana |
| 1.14.19.3 | Y375F | site-directed mutagenesis, mutant shows significantly increased activity compared to the wild-type enzyme | Glossomastix chrysoplasta |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.19.3 | additional information | - |
additional information | Michaelis-Menten kinetics | Glossomastix chrysoplasta | |
| 1.14.19.3 | additional information | - |
additional information | Michaelis-Menten kinetics | Thalassiosira pseudonana |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.14.19.3 | endoplasmic reticulum membrane | a transmembrane enzyme | Glossomastix chrysoplasta | 5789 | - |
| 1.14.19.3 | endoplasmic reticulum membrane | a transmembrane enzyme | Thalassiosira pseudonana | 5789 | - |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.19.3 | alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ | Glossomastix chrysoplasta | - |
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O | - |
? |  |
| 1.14.19.3 | alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ | Thalassiosira pseudonana | - |
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O | - |
? | |
| 1.14.19.3 | linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ | Glossomastix chrysoplasta | - |
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O | - |
? | |
| 1.14.19.3 | linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ | Thalassiosira pseudonana | - |
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.19.3 | Glossomastix chrysoplasta | Q49S39 | - |
- |
| 1.14.19.3 | Thalassiosira pseudonana | Q4G2T1 | - |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 1.14.19.3 | alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O | molecular mechanisms underlying catalytic activity of delta 6 desaturase | Thalassiosira pseudonana | |
| 1.14.19.3 | linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O | molecular mechanisms underlying catalytic activity of delta 6 desaturase | Glossomastix chrysoplasta | |
| 1.14.19.3 | linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O | molecular mechanisms underlying catalytic activity of delta 6 desaturase | Thalassiosira pseudonana |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.19.3 | alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ | - |
Glossomastix chrysoplasta | stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O | - |
? | |
| 1.14.19.3 | alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ | - |
Thalassiosira pseudonana | stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O | - |
? | |
| 1.14.19.3 | alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ | preferred substrate | Glossomastix chrysoplasta | stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O | - |
? | |
| 1.14.19.3 | linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ | - |
Glossomastix chrysoplasta | gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O | - |
? | |
| 1.14.19.3 | linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ | - |
Thalassiosira pseudonana | gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O | - |
? | |
| 1.14.19.3 | linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ | preferred substrate | Thalassiosira pseudonana | gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.19.3 | delta 6 desaturase | - |
Glossomastix chrysoplasta |
| 1.14.19.3 | delta 6 desaturase | - |
Thalassiosira pseudonana |
| 1.14.19.3 | DesI | - |
Thalassiosira pseudonana |
| 1.14.19.3 | FADS2 | - |
Glossomastix chrysoplasta |
| 1.14.19.3 | FADS2 | - |
Thalassiosira pseudonana |
| 1.14.19.3 | GcFADS2 | - |
Glossomastix chrysoplasta |
| 1.14.19.3 | TpFADS2 | - |
Thalassiosira pseudonana |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.14.19.3 | additional information | structure-function relationship, domain-swapping approach, two regions are essential to the catalytic mechanism: one that extends from the end of the fourth to the beginning of the fifth cytoplasmic transmembrane domain, and another that includes the C-terminal region that occurs after the sixth cytoplasmic transmembrane domain. Fatty acid contents of wild-type an dmutant strains, overview | Thalassiosira pseudonana |
| 1.14.19.3 | additional information | structure-function relationship, domain-swapping approach, two regions are essential to the catalytic mechanism: one that extends from the end of the fourth to the beginning of the fifth cytoplasmic transmembrane domain, and another that includes the C-terminal region that occurs after the sixth cytoplasmic transmembrane domain. Fatty acid contents of wild-type and mutant strains, overview | Glossomastix chrysoplasta |
| 1.14.19.3 | physiological function | delta 6 desaturase (FADS2) is a critical bifunctional enzyme required for polyunsaturated fatty acid biosynthesis, high catalytic activity of FADS2s from Glossomastix chrysoplasta. It controls the conversion of linoleoyl-CoA and alpha-linolenoyl-CoA to gamma-linolenic acid and stearidonic acid, respectively | Glossomastix chrysoplasta |
| 1.14.19.3 | physiological function | delta 6 desaturase (FADS2) is a critical bifunctional enzyme required for polyunsaturated fatty acid biosynthesis, high catalytic activity of FADS2s from Thalassiosira pseudonana. It controls the conversion of linoleoyl-CoA and alpha-linolenoyl-CoA to gamma-linolenic acid and stearidonic acid, respectively | Thalassiosira pseudonana |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
