Protein Variants | Comment | Organism |
---|---|---|
D271T | 98% of wild-type activity | Saccharomyces cerevisiae |
F174L | complete loss of activity | Saccharomyces cerevisiae |
H176A | complete loss of activity | Saccharomyces cerevisiae |
H180A | complete loss of activity | Saccharomyces cerevisiae |
H190A | complete loss of activity | Saccharomyces cerevisiae |
H193A | complete loss of activity | Saccharomyces cerevisiae |
H194A | complete loss of activity | Saccharomyces cerevisiae |
H249A | complete loss of activity | Saccharomyces cerevisiae |
H270A | complete loss of activity | Saccharomyces cerevisiae |
H273A | complete loss of activity | Saccharomyces cerevisiae |
H274A | complete loss of activity | Saccharomyces cerevisiae |
L196W | complete loss of activity | Saccharomyces cerevisiae |
additional information | the replacement of any one of conserved His residues of three histidine-rich motifs with an alanine eliminates hydroxylase activity in vivo and in vitro. Residues Phe 174, Asn 182, Ser 191, Leu 196, Pro 199, Asn 266, Tyr 269, Asp 271 and Gln 275 appear to be additionally important elements of the active site but their conversion into corresponding yeast DELTA7-sterol-C5(6)-desaturase Erg3p residues does not lead to a gain in desaturase activity | Saccharomyces cerevisiae |
N182P | complete loss of activity | Saccharomyces cerevisiae |
N266G | complete loss of activity | Saccharomyces cerevisiae |
P199C | complete loss of activity | Saccharomyces cerevisiae |
Q275L | complete loss of activity | Saccharomyces cerevisiae |
S191K | 99% of wild-type activity | Saccharomyces cerevisiae |
Y269C | complete loss of activity | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P38992 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
dihydrosphingosine + NADPH + H+ + O2 | - |
Saccharomyces cerevisiae | phytosphingosine + NADP+ + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
sphingolipid C4-hydroxylase | - |
Saccharomyces cerevisiae |
SUR2 | - |
Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
physiological function | C-4 hydroxylation of sphingolipids is important for the antifungal action of syringomycin E. Mutants with defects in C-4 hydroxylated sphingoid base biosynthesis are resistant to this antifungal agent | Saccharomyces cerevisiae |