BRENDA - Enzyme Database
show all sequences of 1.14.18.5

Structure-function studies of yeast C-4 sphingolipid long chain base hydroxylase

Idkowiak-Baldys, J.; Takemoto, J.Y.; Grilley, M.M.; Biochim. Biophys. Acta 1618, 17-24 (2003)

Data extracted from this reference:

Engineering
Protein Variants
Commentary
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
Organism
UniProt
Commentary
Textmining
Saccharomyces cerevisiae
P38992
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
dihydrosphingosine + NADPH + H+ + O2
-
733375
Saccharomyces cerevisiae
phytosphingosine + NADP+ + H2O
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
sphingolipid C4-hydroxylase
-
Saccharomyces cerevisiae
SUR2
-
Saccharomyces cerevisiae
Engineering (protein specific)
Protein Variants
Commentary
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
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
dihydrosphingosine + NADPH + H+ + O2
-
733375
Saccharomyces cerevisiae
phytosphingosine + NADP+ + H2O
-
-
-
?
General Information
General Information
Commentary
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
General Information (protein specific)
General Information
Commentary
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
Other publictions for EC 1.14.18.5
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
734653
Vacchina
Characterization of bifunction ...
Leishmania major
Mol. Biochem. Parasitol.
184
29-38
2012
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
720322
Moreno-Perez
Sphingolipid base modifying en ...
Helianthus annuus
J. Plant Physiol.
168
831-839
2011
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
719485
Mizutani
Identification of the human sp ...
Homo sapiens
FEBS Lett.
563
93-97
2004
-
-
1
-
-
-
-
-
-
-
2
-
-
5
-
-
-
-
-
5
-
-
3
1
3
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
5
-
-
3
1
-
-
-
-
-
-
-
-
1
1
1
1
-
-
719486
Idkowiak-Baldys
Sphingolipid C4 hydroxylation ...
Saccharomyces cerevisiae
FEBS Lett.
569
272-276
2004
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
721116
Bae
Cloning and functional charact ...
Wickerhamomyces ciferrii
Yeast
21
437-443
2004
-
-
1
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
1
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
733207
Wright
Synthesis of 4-hydroxysphingan ...
Zea mays
Arch. Biochem. Biophys.
415
184-192
2003
-
-
-
-
-
-
-
3
1
-
-
-
-
1
-
-
-
-
-
1
-
-
7
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
1
-
-
-
-
-
-
-
-
1
-
-
7
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
733375
Idkowiak-Baldys
Structure-function studies of ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1618
17-24
2003
-
-
-
-
19
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
19
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
734141
Ternes
Identification and characteriz ...
Mus musculus
J. Biol. Chem.
277
25512-25518
2002
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
719481
Sperling
Functional characterization of ...
Arabidopsis thaliana
FEBS Lett.
494
90-94
2001
-
-
1
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
1
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
719795
Grilley
Syringomycin action gene SYR2 ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae W303C
J. Biol. Chem.
273
11062-11068
1998
-
-
-
-
-
-
-
-
1
1
-
-
-
3
-
-
-
-
-
-
-
-
4
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
719792
Haak
Hydroxylation of Saccharomyces ...
Saccharomyces cerevisiae
J. Biol. Chem.
272
29704-29710
1997
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-