BRENDA - Enzyme Database
show all sequences of 4.2.1.108

Biochemistry and crystal structure of ectoine synthase a metal-containing member of the cupin superfamily

Widderich, N.; Kobus, S.; Hoeppner, A.; Riclea, R.; Seubert, A.; Dickschat, J.S.; Heider, J.; Smits, S.H.; Bremer, E.; PLoS ONE 11, e0151285 (2016)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
gene ectC, sequence comparisons, recombinant expression of a codon-optimized version of C-terminal Strep II-tagged enzyme in Escherichia coli strain BL21 from plasmid pNW12 under control of the tet promoter, which in turn is controlled by the TetR repressor, the genetic expression system can be induced by adding anhydrotetracycline, subcloning in Escherichia coli strain DH5alpha
Sphingopyxis alaskensis
Crystallization (Commentary)
Crystallization (Commentary)
Organism
purified recombinnat Strep II-tagged enzyme, sitting drop vapour diffusion method, mixing of 100 nl of 11 mg/ml enzyme solution with 100 nl of reservoir solution containing 0.05 M, calcium acetate, 0.1 M sodium acetate, pH 4.5, and 40% v/v 1,2-propanediol, and equilibration against 0.05 ml of reservoir solution, or mixing of 0.001 ml of enzyme solution with 0.001 ml of reservoir solution containing 20% w/v PEG 6000, 0.9 M lithium chloride, and 0.1 M citric acid, pH 5.0, 3-10 weeks, X-ray diffraction structure determination and analysis at 1.2 A resolution, modelling
Sphingopyxis alaskensis
Engineering
Protein Variants
Commentary
Organism
C105A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
C105S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
D91A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
D91E
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
Sphingopyxis alaskensis
E115A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
E115D
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
E57A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
E57D
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
F107A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
F107W
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
F107Y
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
H117A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
H51A
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
Sphingopyxis alaskensis
H55A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
H93A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
H93N
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
L87A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
additional information
structure-guided site-directed mutagenesis is used targeting amino acid residues that are evolutionarily highly conserved among the extended EctC protein family, including those forming the presumptive iron-binding site
Sphingopyxis alaskensis
S23A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
T40A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
T41A
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
Sphingopyxis alaskensis
W21A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
Y52A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
Y85A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
Y85F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
Y85W
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten-kinetics
Sphingopyxis alaskensis
4.9
-
(2S)-4-acetamido-2-aminobutanoate
pH 8.5, 15°C, recombinant enzyme
Sphingopyxis alaskensis
25.4
-
N-alpha-acetyl-L-2,4-diaminobutanoate
pH 8.5, 15°C, recombinant enzyme
Sphingopyxis alaskensis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
required, activates 100fold at 1 mM
Sphingopyxis alaskensis
additional information
determination of metal content of recombinant SaEctC protein by ICP-MS. Zn2+ or Co2+ can only weakly substitute for Fe2+. No activation with Ni2+, Mn2+, Cu2+, and Fe3+ at 1 mM
Sphingopyxis alaskensis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
(2S)-4-acetamido-2-aminobutanoate
Sphingopyxis alaskensis
-
L-ectoine + H2O
-
-
?
(2S)-4-acetamido-2-aminobutanoate
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
-
L-ectoine + H2O
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Sphingopyxis alaskensis
Q1GNW6
i.e. Sphingomonas alaskensis
-
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
Q1GNW6
i.e. Sphingomonas alaskensis
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant C-terminal Strep II-tagged enzyme from Escherichia coli by affinity chromatography and gel filtration to homogeneity
Sphingopyxis alaskensis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
(2S)-4-acetamido-2-aminobutanoate
-
749081
Sphingopyxis alaskensis
L-ectoine + H2O
-
-
-
?
(2S)-4-acetamido-2-aminobutanoate
i.e. N-gamma-acetyl-L-2,4-diaminobutanoate
749081
Sphingopyxis alaskensis
L-ectoine + H2O
-
-
-
?
(2S)-4-acetamido-2-aminobutanoate
-
749081
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
L-ectoine + H2O
-
-
-
?
(2S)-4-acetamido-2-aminobutanoate
i.e. N-gamma-acetyl-L-2,4-diaminobutanoate
749081
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
L-ectoine + H2O
-
-
-
?
additional information
EctC not only effectively converts its natural substrate N-gamma-acetyl-L-2,4-diaminobutyric acid into ectoine through a cyclocondensation reaction, but it can also use the isomer N-alpha-acetyl-L-2,4-diaminobutyric acid as its substrate, albeit with substantially reduced catalytic efficiency
749081
Sphingopyxis alaskensis
?
-
-
-
-
additional information
EctC not only effectively converts its natural substrate N-gamma-acetyl-L-2,4-diaminobutyric acid into ectoine through a cyclocondensation reaction, but it can also use the isomer N-alpha-acetyl-L-2,4-diaminobutyric acid as its substrate, albeit with substantially reduced catalytic efficiency
749081
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
?
-
-
-
-
N-alpha-acetyl-L-2,4-diaminobutanoate
-
749081
Sphingopyxis alaskensis
L-ectoine + H2O
-
-
-
?
N-alpha-acetyl-L-2,4-diaminobutanoate
-
749081
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
L-ectoine + H2O
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
-
Sphingopyxis alaskensis
More
overall structure of the open and semi-closed crystal structures of SaEctC, overview
Sphingopyxis alaskensis
Synonyms
Synonyms
Commentary
Organism
(Sa)Ect
-
Sphingopyxis alaskensis
EctC
-
Sphingopyxis alaskensis
L-ectoine synthase
UniProt
Sphingopyxis alaskensis
SaEctC
-
Sphingopyxis alaskensis
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
15
-
recombinant enzyme
Sphingopyxis alaskensis
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.6
-
N-alpha-acetyl-L-2,4-diaminobutanoate
pH 8.5, 15°C, recombinant enzyme
Sphingopyxis alaskensis
7.2
-
(2S)-4-acetamido-2-aminobutanoate
pH 8.5, 15°C, recombinant enzyme
Sphingopyxis alaskensis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
recombinant enzyme
Sphingopyxis alaskensis
Cloned(Commentary) (protein specific)
Commentary
Organism
gene ectC, sequence comparisons, recombinant expression of a codon-optimized version of C-terminal Strep II-tagged enzyme in Escherichia coli strain BL21 from plasmid pNW12 under control of the tet promoter, which in turn is controlled by the TetR repressor, the genetic expression system can be induced by adding anhydrotetracycline, subcloning in Escherichia coli strain DH5alpha
Sphingopyxis alaskensis
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified recombinnat Strep II-tagged enzyme, sitting drop vapour diffusion method, mixing of 100 nl of 11 mg/ml enzyme solution with 100 nl of reservoir solution containing 0.05 M, calcium acetate, 0.1 M sodium acetate, pH 4.5, and 40% v/v 1,2-propanediol, and equilibration against 0.05 ml of reservoir solution, or mixing of 0.001 ml of enzyme solution with 0.001 ml of reservoir solution containing 20% w/v PEG 6000, 0.9 M lithium chloride, and 0.1 M citric acid, pH 5.0, 3-10 weeks, X-ray diffraction structure determination and analysis at 1.2 A resolution, modelling
Sphingopyxis alaskensis
Engineering (protein specific)
Protein Variants
Commentary
Organism
C105A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
C105S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
D91A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
D91E
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
Sphingopyxis alaskensis
E115A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
E115D
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
E57A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
E57D
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
F107A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
F107W
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
F107Y
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
H117A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
H51A
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
Sphingopyxis alaskensis
H55A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
H93A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
H93N
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
L87A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
additional information
structure-guided site-directed mutagenesis is used targeting amino acid residues that are evolutionarily highly conserved among the extended EctC protein family, including those forming the presumptive iron-binding site
Sphingopyxis alaskensis
S23A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
T40A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
T41A
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
Sphingopyxis alaskensis
W21A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
Y52A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
Y85A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
Y85F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
Y85W
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten-kinetics
Sphingopyxis alaskensis
4.9
-
(2S)-4-acetamido-2-aminobutanoate
pH 8.5, 15°C, recombinant enzyme
Sphingopyxis alaskensis
25.4
-
N-alpha-acetyl-L-2,4-diaminobutanoate
pH 8.5, 15°C, recombinant enzyme
Sphingopyxis alaskensis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
required, activates 100fold at 1 mM
Sphingopyxis alaskensis
additional information
determination of metal content of recombinant SaEctC protein by ICP-MS. Zn2+ or Co2+ can only weakly substitute for Fe2+. No activation with Ni2+, Mn2+, Cu2+, and Fe3+ at 1 mM
Sphingopyxis alaskensis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
(2S)-4-acetamido-2-aminobutanoate
Sphingopyxis alaskensis
-
L-ectoine + H2O
-
-
?
(2S)-4-acetamido-2-aminobutanoate
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
-
L-ectoine + H2O
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant C-terminal Strep II-tagged enzyme from Escherichia coli by affinity chromatography and gel filtration to homogeneity
Sphingopyxis alaskensis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
(2S)-4-acetamido-2-aminobutanoate
-
749081
Sphingopyxis alaskensis
L-ectoine + H2O
-
-
-
?
(2S)-4-acetamido-2-aminobutanoate
i.e. N-gamma-acetyl-L-2,4-diaminobutanoate
749081
Sphingopyxis alaskensis
L-ectoine + H2O
-
-
-
?
(2S)-4-acetamido-2-aminobutanoate
-
749081
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
L-ectoine + H2O
-
-
-
?
(2S)-4-acetamido-2-aminobutanoate
i.e. N-gamma-acetyl-L-2,4-diaminobutanoate
749081
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
L-ectoine + H2O
-
-
-
?
additional information
EctC not only effectively converts its natural substrate N-gamma-acetyl-L-2,4-diaminobutyric acid into ectoine through a cyclocondensation reaction, but it can also use the isomer N-alpha-acetyl-L-2,4-diaminobutyric acid as its substrate, albeit with substantially reduced catalytic efficiency
749081
Sphingopyxis alaskensis
?
-
-
-
-
additional information
EctC not only effectively converts its natural substrate N-gamma-acetyl-L-2,4-diaminobutyric acid into ectoine through a cyclocondensation reaction, but it can also use the isomer N-alpha-acetyl-L-2,4-diaminobutyric acid as its substrate, albeit with substantially reduced catalytic efficiency
749081
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
?
-
-
-
-
N-alpha-acetyl-L-2,4-diaminobutanoate
-
749081
Sphingopyxis alaskensis
L-ectoine + H2O
-
-
-
?
N-alpha-acetyl-L-2,4-diaminobutanoate
-
749081
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
L-ectoine + H2O
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
-
Sphingopyxis alaskensis
More
overall structure of the open and semi-closed crystal structures of SaEctC, overview
Sphingopyxis alaskensis
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
15
-
recombinant enzyme
Sphingopyxis alaskensis
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.6
-
N-alpha-acetyl-L-2,4-diaminobutanoate
pH 8.5, 15°C, recombinant enzyme
Sphingopyxis alaskensis
7.2
-
(2S)-4-acetamido-2-aminobutanoate
pH 8.5, 15°C, recombinant enzyme
Sphingopyxis alaskensis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
recombinant enzyme
Sphingopyxis alaskensis
General Information
General Information
Commentary
Organism
evolution
the enzyme is a metal-containing member of the cupin superfamily. Cupins contain two conserved motifs: G(X)5HXH(X)3,4E(X)6G and G(X)5PXG(X)2H(X)3N (the letters in bold represent those residues that often coordinate the metal)
Sphingopyxis alaskensis
metabolism
synthesis of ectoine occurs from the intermediate metabolite L-aspartate-beta-semialdehyde and comprises the sequential activities of three enzymes: L-2,4-diaminobutyrate transaminase (EctB, EC 2.6.1.76), 2,4-diaminobutyrate acetyltransferase (EctA, EC 2.3.1.178), and ectoine synthase (EctC, EC 4.2.1.108)
Sphingopyxis alaskensis
General Information (protein specific)
General Information
Commentary
Organism
evolution
the enzyme is a metal-containing member of the cupin superfamily. Cupins contain two conserved motifs: G(X)5HXH(X)3,4E(X)6G and G(X)5PXG(X)2H(X)3N (the letters in bold represent those residues that often coordinate the metal)
Sphingopyxis alaskensis
metabolism
synthesis of ectoine occurs from the intermediate metabolite L-aspartate-beta-semialdehyde and comprises the sequential activities of three enzymes: L-2,4-diaminobutyrate transaminase (EctB, EC 2.6.1.76), 2,4-diaminobutyrate acetyltransferase (EctA, EC 2.3.1.178), and ectoine synthase (EctC, EC 4.2.1.108)
Sphingopyxis alaskensis
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.02
-
N-alpha-acetyl-L-2,4-diaminobutanoate
pH 8.5, 15°C, recombinant enzyme
Sphingopyxis alaskensis
1.47
-
(2S)-4-acetamido-2-aminobutanoate
pH 8.5, 15°C, recombinant enzyme
Sphingopyxis alaskensis
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.02
-
N-alpha-acetyl-L-2,4-diaminobutanoate
pH 8.5, 15°C, recombinant enzyme
Sphingopyxis alaskensis
1.47
-
(2S)-4-acetamido-2-aminobutanoate
pH 8.5, 15°C, recombinant enzyme
Sphingopyxis alaskensis
Other publictions for EC 4.2.1.108
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)
749081
Widderich
Biochemistry and crystal stru ...
Sphingopyxis alaskensis, Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
PLoS ONE
11
e0151285
2016
-
-
1
1
26
-
-
3
-
2
-
2
-
7
-
-
1
-
-
-
-
-
8
2
5
1
-
-
2
1
-
-
-
-
-
-
-
-
1
-
1
26
-
-
-
-
3
-
2
-
2
-
-
-
1
-
-
-
-
8
2
1
-
-
2
1
-
-
-
-
2
2
-
2
2
746650
Kobus
Overproduction, crystallizati ...
Sphingopyxis alaskensis, Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
Acta Crystallogr. Sect. F
71
1027-1032
2015
-
-
1
1
-
-
-
-
-
-
1
2
-
7
-
-
1
-
-
-
-
-
2
1
4
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
2
-
-
-
1
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
2
2
-
-
-
713911
Witt
Unexpected property of ectoine ...
Halomonas elongata, Halomonas elongata DSM 2581
Appl. Microbiol. Biotechnol.
91
113-122
2011
-
-
1
-
1
-
-
1
-
-
1
2
-
5
-
-
1
-
-
-
2
-
11
1
1
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
1
-
-
1
2
-
-
-
1
-
-
2
-
11
1
1
-
-
-
1
-
-
-
-
3
3
-
-
-
729687
Reshetnikov
Diversity and phylogeny of the ...
Methylarcula marina, Methylarcula marina ML1, Methylobacter marinus, Methylobacter marinus 7C, Methylomicrobium alcaliphilum, Methylomicrobium alcaliphilum ML1, Methylomicrobium kenyense, Methylomicrobium kenyense AMO1, Methylophaga alcalica, Methylophaga alcalica M8, Methylophaga thalassica, Methylophaga thalassica ATCC 33146
Extremophiles
15
653-663
2011
-
-
6
-
-
-
-
-
-
-
-
-
-
19
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
6
-
-
-
690643
Rajan
Characterization and phylogene ...
Bacillus halodurans, Bacillus halodurans TCJAR021
Arch. Microbiol.
190
481-487
2008
-
1
1
-
-
-
-
-
-
-
1
4
-
3
-
-
-
-
-
-
-
-
4
-
1
-
-
-
-
-
-
-
-
-
1
-
-
1
1
-
-
-
-
-
-
-
-
-
-
1
4
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
691437
Rajan
Cloning and heterologous expre ...
Bacillus halodurans, Bacillus halodurans TCJAR021
Biotechnol. Lett.
30
1403-1407
2008
-
1
1
-
-
-
-
-
-
-
1
4
-
3
-
-
-
-
-
-
-
-
4
-
1
-
-
-
-
-
-
-
-
-
1
-
-
1
1
-
-
-
-
-
-
-
-
-
-
1
4
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
660836
Reshetnikov
Characterization of the ectoin ...
Methylomicrobium alcaliphilum
Arch. Microbiol.
184
286-297
2006
1
-
1
-
-
-
-
-
-
1
-
1
-
3
-
-
-
-
-
1
-
-
2
-
1
1
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
1
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
660740
Kuhlmann
Osmotically regulated synthesi ...
Bacillus alcalophilus, Chromohalobacter salexigens, no activity in Aneurinibacillus aneurinilyticus, no activity in Aneurinibacillus aneurinilyticus DSM 5562, no activity in Bacillus cereus, no activity in Bacillus cereus DSM 31, no activity in Bacillus circulans, no activity in Bacillus licheniformis, no activity in Bacillus megaterium, no activity in Bacillus subtilis, no activity in Bacillus subtilis JH642, no activity in Bacillus thuringiensis, no activity in Paenibacillus polymyxa, Sporosarcina pasteurii, Sporosarcina psychrophila, Virgibacillus pantothenticus, Virgibacillus salexigens
Appl. Environ. Microbiol.
68
772-783
2002
6
-
2
-
-
-
-
-
-
1
-
12
-
27
-
-
-
-
-
-
-
-
18
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
2
-
-
-
-
-
-
-
-
-
1
-
12
-
-
-
-
-
-
-
-
18
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
663114
Nakayama
Ectoine, the compatible solute ...
Halomonas elongata, Halomonas elongata OUT30018, no activity in Nicotiana tabacum
Plant Physiol.
122
1239-1247
2000
-
-
1
-
1
-
-
-
-
-
-
2
-
9
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
640091
Ono
Characterization of biosynthet ...
Halomonas elongata, Halomonas elongata OUT30018
J. Bacteriol.
181
91-99
1999
-
-
-
-
-
1
-
2
-
2
2
3
-
5
-
-
1
-
-
-
1
-
6
1
-
3
1
1
-
1
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
2
-
2
2
3
-
-
-
1
-
-
1
-
6
1
3
1
1
-
1
-
-
1
-
-
-
-
-
-
662773
Louis
Characterization of genes for ...
Marinococcus halophilus
Microbiology
143
1141-1149
1997
1
1
1
-
-
-
-
-
-
-
-
2
-
3
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
640090
Peters
-
The biosynthesis of ectoine ...
Halomonas elongata, Halorhodospira halochloris
FEMS Microbiol. Lett.
71
157-162
1990
-
-
-
-
-
-
-
-
-
-
-
2
-
2
-
-
-
-
-
2
-
-
4
-
-
2
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
2
-
-
4
-
2
-
-
-
2
-
-
-
-
-
-
-
-
-