BRENDA - Enzyme Database

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)
EC Number
Cloned (Commentary)
Organism
4.2.1.108
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)
EC Number
Crystallization (Commentary)
Organism
4.2.1.108
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
EC Number
Protein Variants
Commentary
Organism
4.2.1.108
C105A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
C105S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
D91A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
D91E
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
E115A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
E115D
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
E57A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
E57D
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
F107A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
F107W
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
F107Y
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
H117A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
H51A
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
H55A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
H93A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
H93N
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
L87A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
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
4.2.1.108
S23A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
T40A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
T41A
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
W21A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
Y52A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
Y85A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
Y85F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
Y85W
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
4.2.1.108
additional information
-
additional information
Michaelis-Menten-kinetics
Sphingopyxis alaskensis
4.2.1.108
4.9
-
(2S)-4-acetamido-2-aminobutanoate
pH 8.5, 15°C, recombinant enzyme
Sphingopyxis alaskensis
4.2.1.108
25.4
-
N-alpha-acetyl-L-2,4-diaminobutanoate
pH 8.5, 15°C, recombinant enzyme
Sphingopyxis alaskensis
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
4.2.1.108
Fe2+
required, activates 100fold at 1 mM
Sphingopyxis alaskensis
4.2.1.108
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)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
4.2.1.108
(2S)-4-acetamido-2-aminobutanoate
Sphingopyxis alaskensis
-
L-ectoine + H2O
-
-
?
4.2.1.108
(2S)-4-acetamido-2-aminobutanoate
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
-
L-ectoine + H2O
-
-
?
Organism
EC Number
Organism
UniProt
Commentary
Textmining
4.2.1.108
Sphingopyxis alaskensis
Q1GNW6
i.e. Sphingomonas alaskensis
-
4.2.1.108
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
Q1GNW6
i.e. Sphingomonas alaskensis
-
Purification (Commentary)
EC Number
Purification (Commentary)
Organism
4.2.1.108
recombinant C-terminal Strep II-tagged enzyme from Escherichia coli by affinity chromatography and gel filtration to homogeneity
Sphingopyxis alaskensis
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
4.2.1.108
(2S)-4-acetamido-2-aminobutanoate
-
749081
Sphingopyxis alaskensis
L-ectoine + H2O
-
-
-
?
4.2.1.108
(2S)-4-acetamido-2-aminobutanoate
i.e. N-gamma-acetyl-L-2,4-diaminobutanoate
749081
Sphingopyxis alaskensis
L-ectoine + H2O
-
-
-
?
4.2.1.108
(2S)-4-acetamido-2-aminobutanoate
-
749081
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
L-ectoine + H2O
-
-
-
?
4.2.1.108
(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
-
-
-
?
4.2.1.108
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
?
-
-
-
-
4.2.1.108
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
?
-
-
-
-
4.2.1.108
N-alpha-acetyl-L-2,4-diaminobutanoate
-
749081
Sphingopyxis alaskensis
L-ectoine + H2O
-
-
-
?
4.2.1.108
N-alpha-acetyl-L-2,4-diaminobutanoate
-
749081
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
L-ectoine + H2O
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
4.2.1.108
dimer
-
Sphingopyxis alaskensis
4.2.1.108
More
overall structure of the open and semi-closed crystal structures of SaEctC, overview
Sphingopyxis alaskensis
Synonyms
EC Number
Synonyms
Commentary
Organism
4.2.1.108
(Sa)Ect
-
Sphingopyxis alaskensis
4.2.1.108
EctC
-
Sphingopyxis alaskensis
4.2.1.108
L-ectoine synthase
UniProt
Sphingopyxis alaskensis
4.2.1.108
SaEctC
-
Sphingopyxis alaskensis
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
4.2.1.108
15
-
recombinant enzyme
Sphingopyxis alaskensis
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.2.1.108
0.6
-
N-alpha-acetyl-L-2,4-diaminobutanoate
pH 8.5, 15°C, recombinant enzyme
Sphingopyxis alaskensis
4.2.1.108
7.2
-
(2S)-4-acetamido-2-aminobutanoate
pH 8.5, 15°C, recombinant enzyme
Sphingopyxis alaskensis
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
4.2.1.108
8.5
-
recombinant enzyme
Sphingopyxis alaskensis
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
4.2.1.108
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)
EC Number
Crystallization
Organism
4.2.1.108
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)
EC Number
Protein Variants
Commentary
Organism
4.2.1.108
C105A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
C105S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
D91A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
D91E
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
E115A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
E115D
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
E57A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
E57D
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
F107A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
F107W
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
F107Y
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
H117A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
H51A
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
H55A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
H93A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
H93N
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
L87A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
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
4.2.1.108
S23A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
T40A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
T41A
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
W21A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
Y52A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
Y85A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
Y85F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
4.2.1.108
Y85W
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Sphingopyxis alaskensis
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
4.2.1.108
additional information
-
additional information
Michaelis-Menten-kinetics
Sphingopyxis alaskensis
4.2.1.108
4.9
-
(2S)-4-acetamido-2-aminobutanoate
pH 8.5, 15°C, recombinant enzyme
Sphingopyxis alaskensis
4.2.1.108
25.4
-
N-alpha-acetyl-L-2,4-diaminobutanoate
pH 8.5, 15°C, recombinant enzyme
Sphingopyxis alaskensis
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
4.2.1.108
Fe2+
required, activates 100fold at 1 mM
Sphingopyxis alaskensis
4.2.1.108
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)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
4.2.1.108
(2S)-4-acetamido-2-aminobutanoate
Sphingopyxis alaskensis
-
L-ectoine + H2O
-
-
?
4.2.1.108
(2S)-4-acetamido-2-aminobutanoate
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
-
L-ectoine + H2O
-
-
?
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
4.2.1.108
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)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
4.2.1.108
(2S)-4-acetamido-2-aminobutanoate
-
749081
Sphingopyxis alaskensis
L-ectoine + H2O
-
-
-
?
4.2.1.108
(2S)-4-acetamido-2-aminobutanoate
i.e. N-gamma-acetyl-L-2,4-diaminobutanoate
749081
Sphingopyxis alaskensis
L-ectoine + H2O
-
-
-
?
4.2.1.108
(2S)-4-acetamido-2-aminobutanoate
-
749081
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
L-ectoine + H2O
-
-
-
?
4.2.1.108
(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
-
-
-
?
4.2.1.108
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
?
-
-
-
-
4.2.1.108
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
?
-
-
-
-
4.2.1.108
N-alpha-acetyl-L-2,4-diaminobutanoate
-
749081
Sphingopyxis alaskensis
L-ectoine + H2O
-
-
-
?
4.2.1.108
N-alpha-acetyl-L-2,4-diaminobutanoate
-
749081
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
L-ectoine + H2O
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
4.2.1.108
dimer
-
Sphingopyxis alaskensis
4.2.1.108
More
overall structure of the open and semi-closed crystal structures of SaEctC, overview
Sphingopyxis alaskensis
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
4.2.1.108
15
-
recombinant enzyme
Sphingopyxis alaskensis
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.2.1.108
0.6
-
N-alpha-acetyl-L-2,4-diaminobutanoate
pH 8.5, 15°C, recombinant enzyme
Sphingopyxis alaskensis
4.2.1.108
7.2
-
(2S)-4-acetamido-2-aminobutanoate
pH 8.5, 15°C, recombinant enzyme
Sphingopyxis alaskensis
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
4.2.1.108
8.5
-
recombinant enzyme
Sphingopyxis alaskensis
General Information
EC Number
General Information
Commentary
Organism
4.2.1.108
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
4.2.1.108
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)
EC Number
General Information
Commentary
Organism
4.2.1.108
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
4.2.1.108
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]
EC Number
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
4.2.1.108
0.02
-
N-alpha-acetyl-L-2,4-diaminobutanoate
pH 8.5, 15°C, recombinant enzyme
Sphingopyxis alaskensis
4.2.1.108
1.47
-
(2S)-4-acetamido-2-aminobutanoate
pH 8.5, 15°C, recombinant enzyme
Sphingopyxis alaskensis
KCat/KM [mM/s] (protein specific)
EC Number
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
4.2.1.108
0.02
-
N-alpha-acetyl-L-2,4-diaminobutanoate
pH 8.5, 15°C, recombinant enzyme
Sphingopyxis alaskensis
4.2.1.108
1.47
-
(2S)-4-acetamido-2-aminobutanoate
pH 8.5, 15°C, recombinant enzyme
Sphingopyxis alaskensis