Cloned (Comment) | Organism |
---|---|
gene RKD12, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time PCR enzyme expression analysis, recombinant expression in Saccharomyces cerevisiae | Rhodotorula kratochvilovae |
RKD12 is further transformed into Saccharomyces cerevisiae for functional characterization | Rhodotorula kratochvilovae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
a 1-oleoyl-2-acyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ | Rhodotorula kratochvilovae | - |
a 1-linoleoyl-2-acyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O | - |
? | |
additional information | Rhodotorula kratochvilovae | the enzyme produces linoleic acid and alpha-linolenic acid, overview | ? | - |
? | |
additional information | Rhodotorula kratochvilovae YM25235 | the enzyme produces linoleic acid and alpha-linolenic acid, overview | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodotorula kratochvilovae | A0A024B710 | - |
- |
Rhodotorula kratochvilovae | A0A024B710 | isolated from Chenghai Lake in Yunnan, China | - |
Rhodotorula kratochvilovae YM25235 | A0A024B710 | - |
- |
Rhodotorula kratochvilovae YM25235 | A0A024B710 | isolated from Chenghai Lake in Yunnan, China | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
a 1-oleoyl-2-acyl-[glycerolipid] + 2 reduced ferredoxin [iron-sulfur] cluster + O2 + 2 H+ | - |
Rhodotorula kratochvilovae | a 1-linoleoyl-2-acyl-[glycerolipid] + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H2O | - |
? | |
additional information | the enzyme produces linoleic acid and alpha-linolenic acid, overview | Rhodotorula kratochvilovae | ? | - |
? | |
additional information | absence of desaturation activity of RKD12 for C16 substrates | Rhodotorula kratochvilovae | ? | - |
? | |
additional information | the enzyme produces linoleic acid and alpha-linolenic acid, overview | Rhodotorula kratochvilovae YM25235 | ? | - |
? | |
additional information | absence of desaturation activity of RKD12 for C16 substrates | Rhodotorula kratochvilovae YM25235 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 50600, about, sequence calculation | Rhodotorula kratochvilovae |
? | x * 50634, calculated from sequence | Rhodotorula kratochvilovae |
Synonyms | Comment | Organism |
---|---|---|
bifunctional DELTA12/DELTA15-fatty acid desaturase | - |
Rhodotorula kratochvilovae |
DELTA(12) fatty acid desaturase | - |
Rhodotorula kratochvilovae |
DELTA12-desaturase | - |
Rhodotorula kratochvilovae |
More | cf. EC 1.14.19.13 | Rhodotorula kratochvilovae |
RKD12 | - |
Rhodotorula kratochvilovae |
RKD12 | bifunctional DELTA12/DELTA15-desaturase gene | Rhodotorula kratochvilovae |
Organism | Comment | Expression |
---|---|---|
Rhodotorula kratochvilovae | a culture temperature downshift from 28°C to 15°C induces the enzyme | up |
General Information | Comment | Organism |
---|---|---|
evolution | bifunctional DELTA12/DELTA15-desaturases are widely found in fungi species belonging to Ascomycota and Basidiomycota. Enzyme RKD12 shares higher homology to the Cop-odeA, it only exhibits DELTA12 and DELTA15 desaturation activity on C18 substrates without preference | Rhodotorula kratochvilovae |
physiological function | for better adaptation to low temperatures, YM25235 may have evolved some adaptative mechanisms that might include the alteration of unsaturation levels of fatty acids in membrane lipids involving th enzyme | Rhodotorula kratochvilovae |
physiological function | increased RKD12 mRNA expression level and PUFAs content at low temperature might be helpful for the cold adaptation of Rhodosporidium kratochvilovae YM25235 | Rhodotorula kratochvilovae |