BRENDA - Enzyme Database
show all sequences of 1.14.19.46

Mutation study of conserved amino acid residues of Spirulina DELTA6-acyl-lipid desaturase showing involvement of histidine 313 in the regioselectivity of the enzyme

Hongsthong, A.; Subudhi, S.; Sirijuntarat, M.; Cheevadhanarak, S.; Appl. Microbiol. Biotechnol. 66, 74-84 (2004)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli DH5alpha cells
Arthrospira platensis
Engineering
Amino acid exchange
Commentary
Organism
D138N
inactive
Arthrospira platensis
E140Q
inactive
Arthrospira platensis
G136H
inactive
Arthrospira platensis
H124R
inactive
Arthrospira platensis
H128R
inactive
Arthrospira platensis
H129R
inactive
Arthrospira platensis
H305R
the mutant shows 17% of wild type activity
Arthrospira platensis
H306R
inactive
Arthrospira platensis
H313R
inactive
Arthrospira platensis
H315N
inactive
Arthrospira platensis
H89R
inactive
Arthrospira platensis
H93R
the mutant shows 11% of wild type activity
Arthrospira platensis
R123N
the mutant shows 91% of wild type activity
Arthrospira platensis
W294G
inactive
Arthrospira platensis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.5
-
linoleic acid
mutant enzyme R123N, at pH 7.5 and 25C; wild type enzyme, at pH 7.5 and 25C
Arthrospira platensis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
47000
-
x * 47000, SDS-PAGE
Arthrospira platensis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
linoleic acid + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
Arthrospira platensis
-
gamma-linolenic acid + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Arthrospira platensis
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
linoleic acid + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
-
733180
Arthrospira platensis
gamma-linolenic acid + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 47000, SDS-PAGE
Arthrospira platensis
Cofactor
Cofactor
Commentary
Organism
Structure
Ferredoxin
-
Arthrospira platensis
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli DH5alpha cells
Arthrospira platensis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
Ferredoxin
-
Arthrospira platensis
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D138N
inactive
Arthrospira platensis
E140Q
inactive
Arthrospira platensis
G136H
inactive
Arthrospira platensis
H124R
inactive
Arthrospira platensis
H128R
inactive
Arthrospira platensis
H129R
inactive
Arthrospira platensis
H305R
the mutant shows 17% of wild type activity
Arthrospira platensis
H306R
inactive
Arthrospira platensis
H313R
inactive
Arthrospira platensis
H315N
inactive
Arthrospira platensis
H89R
inactive
Arthrospira platensis
H93R
the mutant shows 11% of wild type activity
Arthrospira platensis
R123N
the mutant shows 91% of wild type activity
Arthrospira platensis
W294G
inactive
Arthrospira platensis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.5
-
linoleic acid
mutant enzyme R123N, at pH 7.5 and 25C; wild type enzyme, at pH 7.5 and 25C
Arthrospira platensis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
47000
-
x * 47000, SDS-PAGE
Arthrospira platensis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
linoleic acid + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
Arthrospira platensis
-
gamma-linolenic acid + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
linoleic acid + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
-
733180
Arthrospira platensis
gamma-linolenic acid + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 47000, SDS-PAGE
Arthrospira platensis
Other publictions for EC 1.14.19.46
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
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)
675898
Kurdrid
Effect of two intermediate ele ...
Arthrospira platensis
Mol. Biol. Rep.
34
261-266
2006
2
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
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-
1
-
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2
-
1
1
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1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
733181
Hongsthong
Revealing the complementation ...
Arthrospira platensis
Appl. Microbiol. Biotechnol.
72
1192-1201
2006
-
-
1
-
-
-
-
-
-
-
1
1
-
1
-
-
-
-
-
-
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1
1
-
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1
-
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-
1
1
-
-
-
-
-
-
-
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1
1
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
675896
Kurdrid
Functional expression of Spiru ...
Arthrospira platensis
Mol. Biol. Rep.
32
215-226
2005
-
-
1
-
-
-
-
-
-
-
-
2
-
1
-
-
-
-
-
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2
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1
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1
1
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2
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2
-
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-
-
-
-
-
-
-
-
-
-
-
-
733180
Hongsthong
Mutation study of conserved am ...
Arthrospira platensis
Appl. Microbiol. Biotechnol.
66
74-84
2004
-
-
1
-
14
-
-
1
-
-
1
1
-
1
-
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-
-
-
-
-
1
1
-
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1
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1
1
-
14
-
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1
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1
1
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-
1
1
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-
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-
-
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-
-
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-
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-
733373
Szalontai
Membrane dynamics as seen by f ...
Synechocystis sp.
Biochim. Biophys. Acta
1509
409-419
2000
-
-
-
-
-
-
-
-
1
-
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1
-
1
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-
-
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1
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1
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1
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1
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1
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1
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-
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733718
Tasaka
Targeted mutagenesis of acyl-l ...
Synechocystis sp.
EMBO J.
15
6416-6425
1996
-
-
-
-
-
-
-
-
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1
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1
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1
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1
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1
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1
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1
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