Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.14.19.3 extracted from

  • Shi, H.; Wu, R.; Zheng, Y.; Yue, X.
    Molecular mechanisms underlying catalytic activity of delta 6 desaturase from Glossomastix chrysoplasta and Thalassiosira pseudonana (2017), J. Lipid Res., 59, 79-88 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene D6, recombinant expression in Saccharomyces Glossomastix chrysoplasta
gene desI, recombinant expression in Saccharomyces Thalassiosira pseudonana

Protein Variants

Protein Variants Comment Organism
D313I site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme Glossomastix chrysoplasta
D367H site-directed mutagenesis, mutant shows similar activity compared to the wild-type enzyme Glossomastix chrysoplasta
F310L site-directed mutagenesis, mutant shows similar activity compared to the wild-type enzyme Glossomastix chrysoplasta
H360D site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme Thalassiosira pseudonana
H381N site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme Thalassiosira pseudonana
I306L site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme Thalassiosira pseudonana
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
L303F site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme Thalassiosira pseudonana
L383I site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme Thalassiosira pseudonana
M384S/M385 site-directed mutagenesis, mutant shows reduced activity compared to the wild-type enzyme Thalassiosira pseudonana
M384S/M385L site-directed mutagenesis, mutant shows significantly increased activity compared to the wild-type enzyme Glossomastix chrysoplasta
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
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
N388H site-directed mutagenesis, mutant shows similar activity compared to the wild-type enzyme Glossomastix chrysoplasta
S306T site-directed mutagenesis, mutant shows similar activity compared to the wild-type enzyme Glossomastix chrysoplasta
S322A site-directed mutagenesis, mutant shows reduced activity compared to the wild-type enzyme Thalassiosira pseudonana
S322A site-directed mutagenesis, mutant shows highly increased activity compared to the wild-type enzyme Glossomastix chrysoplasta
T299S site-directed mutagenesis, mutant shows slightly reduced activity compared to the wild-type enzyme Thalassiosira pseudonana
T302V site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Thalassiosira pseudonana
T302V site-directed mutagenesis, mutant shows highly increased activity compared to the wild-type enzyme Glossomastix chrysoplasta
T302V site-directed mutagenesis, mutant shows potently increased activity compared to the wild-type enzyme Glossomastix chrysoplasta
Y375F site-directed mutagenesis, mutant shows reduced activity compared to the wild-type enzyme Thalassiosira pseudonana
Y375F site-directed mutagenesis, mutant shows significantly increased activity compared to the wild-type enzyme Glossomastix chrysoplasta

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics Glossomastix chrysoplasta
additional information
-
additional information Michaelis-Menten kinetics Thalassiosira pseudonana

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum membrane a transmembrane enzyme Glossomastix chrysoplasta 5789
-
endoplasmic reticulum membrane a transmembrane enzyme Thalassiosira pseudonana 5789
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ Glossomastix chrysoplasta
-
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ Thalassiosira pseudonana
-
stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ Glossomastix chrysoplasta
-
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ Thalassiosira pseudonana
-
gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
?

Organism

Organism UniProt Comment Textmining
Glossomastix chrysoplasta Q49S39
-
-
Thalassiosira pseudonana Q4G2T1
-
-

Reaction

Reaction Comment Organism Reaction ID
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
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
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
-
Glossomastix chrysoplasta stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
-
Thalassiosira pseudonana stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
?
alpha-linolenoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ preferred substrate Glossomastix chrysoplasta stearidonoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
-
Glossomastix chrysoplasta gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+
-
Thalassiosira pseudonana gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
?
linoleoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ preferred substrate Thalassiosira pseudonana gamma-linolenoyl-CoA + 2 ferricytochrome b5 + 2 H2O
-
?

Synonyms

Synonyms Comment Organism
delta 6 desaturase
-
Glossomastix chrysoplasta
delta 6 desaturase
-
Thalassiosira pseudonana
DesI
-
Thalassiosira pseudonana
FADS2
-
Glossomastix chrysoplasta
FADS2
-
Thalassiosira pseudonana
GcFADS2
-
Glossomastix chrysoplasta
TpFADS2
-
Thalassiosira pseudonana

General Information

General Information Comment Organism
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
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
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
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