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Enzyme Nomenclature
Information on EC 4.2.1.108 - ectoine synthase
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EC Tree
4.2.1.108 ectoine synthaseIUBMB Comments
Ectoine is an osmoprotectant that is found in halophilic eubacteria. This enzyme is part of the ectoine biosynthesis pathway and only acts in the direction of ectoine formation. cf. EC 3.5.4.44, ectoine hydrolase.
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Word Map
- 4.2.1.108
-
halophil
- acetyltransferase
-
diaminobutyric
- halomonas
-
hydroxyectoine
-
ectabc
- elongata
-
l-2,4-diaminobutyric
-
osmoprotectant
-
methanotrophs
-
halotolerant
-
methylomicrobium
- salexigens
-
osmoregulated
-
paenibacillus
-
sphingopyxis
- lautus
-
cupin
- alcalophilus
-
methylophaga
-
tetrahydropyrimidine
-
nada
-
chromohalobacter
-
osmoadaptation
- 2,4-diaminobutyrate
-
methylobacter
- biotechnology
-
beta-semialdehyde
- virgibacillus
-
non-halophilic
- alaskensis
- industry
The enzyme appears in viruses and cellular organisms
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(Sa)Ect
EctC
ectoine synthase
L-ectoine synthase
SaEctC
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2S)-4-acetamido-2-aminobutanoate = L-ectoine + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
condensation
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
N4-acetyl-L-2,4-diaminobutanoate hydro-lyase (L-ectoine-forming)
Ectoine is an osmoprotectant that is found in halophilic eubacteria. This enzyme is part of the ectoine biosynthesis pathway and only acts in the direction of ectoine formation. cf. EC 3.5.4.44, ectoine hydrolase.
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CAS REGISTRY NUMBER
COMMENTARY
130457-09-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N4-acetyl-L-2,4-diaminobutyrate
2-methyl-1,4,5,6-tetrahydropyrimidine-4-carboxylic acid + H2O
(2S)-4-acetamido-2-aminobutanoate
L-ectoine + H2O
-
i.e. N-gamma-acetyl-L-2,4-diaminobutanoate
-
-
?
(2S)-4-acetamido-2-aminobutanoate
L-ectoine + H2O
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
-
-
-
?
(2S)-4-acetamido-2-aminobutanoate
L-ectoine + H2O
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
-
-
-
-
?
(2S)-4-acetamido-2-aminobutanoate
L-ectoine + H2O
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
-
i.e. N-gamma-acetyl-L-2,4-diaminobutanoate
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
final step in L-ectoine biosynthesis, L-ectoine acts as an osmoprotectant
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
i.e. 1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid
NMR product identification
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
final step in L-ectoine biosynthesis, L-ectoine acts as an osmoprotectant
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
i.e. 1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid
NMR product identification
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
final step in L-ectoine biosynthesis, L-ectoine is the compatible solute in the cell
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
final step in L-ectoine biosynthesis, pathway overview
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
final step in L-ectoine biosynthesis, pathway overview, L-ectoine is the main compatible solute in the organism with a cytoplasmic concentration of 1-2 M
-
-
r
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
i.e. 1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
i.e. 1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid
NMR and thin layer chromatography product identification
-
r
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
i.e. 1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid, circularization, L-ectoine as an effective osmoprotectant, the enzyme shows absolute substrate specificity, reversibility of the reaction is not detected but might be below detection range
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
final step in L-ectoine biosynthesis, pathway overview
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
i.e. 1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid, circularization, L-ectoine as an effective osmoprotectant, the enzyme shows absolute substrate specificity, reversibility of the reaction is not detected but might be below detection range
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
final step in L-ectoine biosynthesis, L-ectoine is the compatible solute in the cell
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
i.e. 1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
final step in L-ectoine biosynthesis, pathway overview
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
i.e. 1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid, circularization, L-ectoine as an effective osmoprotectant, the enzyme shows absolute substrate specificity, reversibility of the reaction is not detected but might be below detection range
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
final step in L-ectoine biosynthesis, pathway overview
-
-
r
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
i.e. 1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid
NMR and TLC product identification
-
r
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
final step in L-ectoine biosynthesis, pathway overview
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
i.e. 1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
final step in L-ectoine biosynthesis, pathway overview
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
i.e. 1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid
NMR product identification
-
r
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
final step in L-ectoine biosynthesis, L-ectoine acts as an osmoprotectant
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
i.e. 1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid
NMR identification
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
final step in L-ectoine biosynthesis, L-ectoine acts as an osmoprotectant
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
i.e. 1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid
NMR identification
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
final step in L-ectoine biosynthesis, L-ectoine acts as an osmoprotectant
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
i.e. 1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid
NMR product identification
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
final step in L-ectoine biosynthesis, L-ectoine acts as an osmoprotectant
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
i.e. 1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid
NMR product identification
-
?
D,L-4,5-dihydro-2-methylimidazole-4-carboxylate + H2O
?
-
-
-
-
r
L-glutamine
5-amino-3,4-dihydro-2H-pyrrole-2-carboxylate + H2O
-
-
-
-
r
N-alpha-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
-
-
-
-
?
N4-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
an intramolecular condensation reaction
i.e. 1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid, over 95% conversion by the recombinant ectoine synthase
-
r
N4-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
an intramolecular condensation reaction
i.e. 1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid, over 95% conversion by the recombinant ectoine synthase
-
r
N4-acetyl-L-2,4-diaminobutyrate
2-methyl-1,4,5,6-tetrahydropyrimidine-4-carboxylic acid + H2O
-
-
-
?
N4-acetyl-L-2,4-diaminobutyrate
2-methyl-1,4,5,6-tetrahydropyrimidine-4-carboxylic acid + H2O
-
-
-
?
N4-acetyl-L-2,4-diaminobutyrate
L-ectoine + H2O
-
-
-
?
additional information
?
-
-
ectoine synthase accepts more than one substrate and is a reversible enzyme able to catalyze both the intramolecular condensation into and the hydrolytic cleavage of cyclic amino acid derivatives. It forms 5-amino-3,4-dihydro-2H-pyrrole-2-carboxylate, ADPC, by cyclic condensation of glutamine in a reversible reaction. A number of ectoine derivatives, in particular 4,5-dihydro-2-methylimidazole-4-carboxylate and L-homoectoine, are also cleaved by ectoine synthase. Proposed reaction mechanism leading to L-ectoine and 5-amino-3,4-dihydro-2H-pyrrole-2-carboxylate, respectively, catalyzed by ectoine synthase, overview
-
-
-
additional information
?
-
-
ectoine synthase accepts more than one substrate and is a reversible enzyme able to catalyze both the intramolecular condensation into and the hydrolytic cleavage of cyclic amino acid derivatives. It forms 5-amino-3,4-dihydro-2H-pyrrole-2-carboxylate, ADPC, by cyclic condensation of glutamine in a reversible reaction. A number of ectoine derivatives, in particular 4,5-dihydro-2-methylimidazole-4-carboxylate and L-homoectoine, are also cleaved by ectoine synthase. Proposed reaction mechanism leading to L-ectoine and 5-amino-3,4-dihydro-2H-pyrrole-2-carboxylate, respectively, catalyzed by ectoine synthase, overview
-
-
-
additional information
?
-
-
the enzyme is osmoregulated in response to medium salinity allowing the organism to live in environments with high concentration of osmolytes
-
-
-
additional information
?
-
the enzyme is osmoregulated in response to medium salinity allowing the organism to live in environments with high concentration of osmolytes
-
-
-
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
-
-
-
additional information
?
-
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
-
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
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N4-acetyl-L-2,4-diaminobutyrate
2-methyl-1,4,5,6-tetrahydropyrimidine-4-carboxylic acid + H2O
(2S)-4-acetamido-2-aminobutanoate
L-ectoine + H2O
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
-
-
-
?
(2S)-4-acetamido-2-aminobutanoate
L-ectoine + H2O
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
-
-
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
final step in L-ectoine biosynthesis, L-ectoine acts as an osmoprotectant
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
final step in L-ectoine biosynthesis, L-ectoine acts as an osmoprotectant
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
final step in L-ectoine biosynthesis, L-ectoine is the compatible solute in the cell
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
final step in L-ectoine biosynthesis, pathway overview
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
final step in L-ectoine biosynthesis, pathway overview, L-ectoine is the main compatible solute in the organism with a cytoplasmic concentration of 1-2 M
-
-
r
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
final step in L-ectoine biosynthesis, pathway overview
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
final step in L-ectoine biosynthesis, L-ectoine is the compatible solute in the cell
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
final step in L-ectoine biosynthesis, pathway overview
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
final step in L-ectoine biosynthesis, pathway overview
-
-
r
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
final step in L-ectoine biosynthesis, pathway overview
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
final step in L-ectoine biosynthesis, pathway overview
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
final step in L-ectoine biosynthesis, L-ectoine acts as an osmoprotectant
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
final step in L-ectoine biosynthesis, L-ectoine acts as an osmoprotectant
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
final step in L-ectoine biosynthesis, L-ectoine acts as an osmoprotectant
-
-
?
4-N-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
final step in L-ectoine biosynthesis, L-ectoine acts as an osmoprotectant
-
-
?
N4-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
an intramolecular condensation reaction
-
-
r
N4-acetyl-L-2,4-diaminobutanoate
L-ectoine + H2O
-
an intramolecular condensation reaction
-
-
r
N4-acetyl-L-2,4-diaminobutyrate
2-methyl-1,4,5,6-tetrahydropyrimidine-4-carboxylic acid + H2O
-
-
-
?
N4-acetyl-L-2,4-diaminobutyrate
2-methyl-1,4,5,6-tetrahydropyrimidine-4-carboxylic acid + H2O
-
-
-
?
N4-acetyl-L-2,4-diaminobutyrate
L-ectoine + H2O
-
-
-
?
additional information
?
-
-
the enzyme is osmoregulated in response to medium salinity allowing the organism to live in environments with high concentration of osmolytes
-
-
-
additional information
?
-
the enzyme is osmoregulated in response to medium salinity allowing the organism to live in environments with high concentration of osmolytes
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
NaCl
additional information
additional information
-
the enzyme is not affected by Mg2+, Ca2+, Mn2+, Li+, K+, and NH4+
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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
high osmolarity induces the enzyme expression, requirements
-
additional information
high osmolarity induces the enzyme expression, requirements
-
additional information
-
high salinity/osmolarity of the medium induces enzyme expression
-
additional information
high salinity/osmolarity of the medium induces enzyme expression
-
additional information
enzyme expression is 12fold induced by NaCl at 1 M
-
additional information
high osmolarity induces the enzyme expression, requirements
-
additional information
-
high osmolarity induces the enzyme expression, requirements
-
additional information
-
high osmolarity induces the enzyme expression, requirements
-
additional information
-
high osmolarity induces the enzyme expression, requirements
-
additional information
-
high osmolarity induces the enzyme expression, requirements
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.9
(2S)-4-acetamido-2-aminobutanoate
-
pH 8.5, 15°C, recombinant enzyme
25.4
N-alpha-acetyl-L-2,4-diaminobutanoate
-
pH 8.5, 15°C, recombinant enzyme
additional information
additional information
-
Michaelis-Menten-kinetics
-
8.4
4-N-acetyl-L-2,4-diaminobutanoate
-
pH 9.5, 15°C, in presence of 0.77 M NaCl
11
4-N-acetyl-L-2,4-diaminobutanoate
-
pH 9.5, 15°C, in presence of 0.05 M NaCl
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.2
(2S)-4-acetamido-2-aminobutanoate
-
pH 8.5, 15°C, recombinant enzyme
0.6
N-alpha-acetyl-L-2,4-diaminobutanoate
-
pH 8.5, 15°C, recombinant enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.47
(2S)-4-acetamido-2-aminobutanoate
-
pH 8.5, 15°C, recombinant enzyme
0.02
N-alpha-acetyl-L-2,4-diaminobutanoate
-
pH 8.5, 15°C, recombinant enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.16
-
purified recombinant enzyme, substrate is 4,5-dihydro-2-methylimidazole-4-carboxylate, hydrolytic reaction, pH 8.5, 21°C
0.3
-
purified recombinant enzyme, substrate is 5-amino-3,4-dihydro-2H-pyrrole-2-carboxylate, hydrolytic reaction, pH 8.5, 21°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 30
-
the temperature optimum shifts from 0°C to 30°C with increasing NaCl concentration
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
formerly Halomonas elongata, strain DSM 3043, gene ectC encoded in the ectABC gene cluster
SwissProt
brenda
i.e. Methylobacter alcaliphilus, gene ectC
UniProt
brenda
no activity in Aneurinibacillus aneurinilyticus DSM 5562
formerly Bacillus aneurinilyticus
-
-
brenda
strain DSM 33, gene ectC encoded in the ectABC gene cluster
SwissProt
brenda
the ectABC gene cluster expressed in Escherichia coli M15 (pREP4)
TrEMBL
brenda
the ectABC gene cluster expressed in Escherichia coli M15 (pREP4)
TrEMBL
brenda
ectABCask gene cluster sequence; 20Z, obligate methanotroph, gene ectC
SwissProt
brenda
i.e. Methylobacter alcaliphilus, gene ectC
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
cells are grown in an atmosphere of air-methane 1:1 in 1 M NaCl
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
evolution
-
ectoine biosynthetic genes (ectABC) are widely distributed in bacteria, ectoine synthase is a member of the cupin superfamily
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)
evolution
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
-
ectoine biosynthetic genes (ectABC) are widely distributed in bacteria, ectoine synthase is a member of the cupin superfamily; 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)
-
malfunction
-
in Halomonas elongata mutant strains deficient in ectA, encoding L-2,4-diaminobutyric acid acetyltransferase, no ectoine synthesis is obeserved
malfunction
-
in Halomonas elongata mutant strains deficient in ectA, encoding L-2,4-diaminobutyric acid acetyltransferase, no ectoine synthesis is obeserved
-
metabolism
-
ectoine synthase is involved in the biosynthetic pathway of L-ectoine and (S,S)-beta-hydroxyectoine, involvement of ectoine synthase in 5-amino-3,4-dihydro-2H-pyrrole-2-carboxylate biosynthesis in vitro
metabolism
the enzyme is involved in ectoine biosynthesis
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)
metabolism
-
ectoine synthase is involved in the biosynthetic pathway of L-ectoine and (S,S)-beta-hydroxyectoine, involvement of ectoine synthase in 5-amino-3,4-dihydro-2H-pyrrole-2-carboxylate biosynthesis in vitro
-
metabolism
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
-
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)
-
physiological function
-
extraordinary protective properties of 5-amino-3,4-dihydro-2H-pyrrole-2-carboxylate produced by ectoine synthase
physiological function
-
microorganisms that carry the ectoine biosynthetic genes (ectABC) make copious amounts of ectoine as a cell protectant in response to high-osmolarity challenges. Ectoine synthase (EctC) is the key enzyme for the production of this compatible solute and mediates the last step of ectoine biosynthesis. It catalyzes the ring closure of the cyclic ectoine molecule
physiological function
-
extraordinary protective properties of 5-amino-3,4-dihydro-2H-pyrrole-2-carboxylate produced by ectoine synthase
-
physiological function
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
-
microorganisms that carry the ectoine biosynthetic genes (ectABC) make copious amounts of ectoine as a cell protectant in response to high-osmolarity challenges. Ectoine synthase (EctC) is the key enzyme for the production of this compatible solute and mediates the last step of ectoine biosynthesis. It catalyzes the ring closure of the cyclic ectoine molecule
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
additional information
-
overall structure of the open and semi-closed crystal structures of SaEctC, overview
additional information
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
-
overall structure of the open and semi-closed crystal structures of SaEctC, overview
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant 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, 12°C, ten weeks, X-ray diffraction structure determination and analysis at 1.0 A resolution, molecular replacement using the crystal structure of Zn2+-containing cupin RemF from Streptomyces resistomycificus (PDB ID 3ht1) as template
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C105A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
C105S
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D91A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D91E
-
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
E115A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E115D
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E57A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E57D
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F107A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F107W
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F107Y
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H117A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H51A
-
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
H55A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H93A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H93N
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L87A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S23A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T40A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T41A
-
site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme
W21A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y52A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y85A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y85F
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y85W
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
C105A
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
C105S
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
E57A
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
H117A
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
additional information
additional information
-
expression in transgenic Nicotiana tabacum BY2 cells increases the osmotolerance and growth rate of the cells under hyperosmotic conditions
additional information
-
construction of enzyme-deficient strains by gene ectC inframe deletion though the splicing-by-overlap-extension PCR technique
additional information
-
construction of enzyme-deficient strains by gene ectC inframe deletion though the splicing-by-overlap-extension PCR technique
-
additional information
-
expression in transgenic Nicotiana tabacum BY2 cells increases the osmotolerance and growth rate of the cells under hyperosmotic conditions
-
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
additional information
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
-
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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme by ammonium sulfate fractionation, hydrophobic interaction chromatography, ultrafiltration, and hydroxylapatite chromatography, in presence of 1 mM L-2,4-diaminobutanoate and over 2 M NaCl to homogeneity
-
recombinant C-terminal Strep II-tagged enzyme from Escherichia coli by affinity chromatography and gel filtration to homogeneity
-
recombinant C-terminall Strep II-tagged enzyme from Escherichia coli by affinity chromatography and gel filtration to homogeneity
-
recombinant His6-tagged ectoine synthase from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His6-tagged ectoine synthase in Escherichia coli strain BL21(DE3)
-
functional expression in transgenic Nicotiana tabaccum BY2 cells using the Agrobacterium tumefaciens infection system
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gene ectC encoded in the ectABC gene cluster, functional expression in Escherichia coli
gene ectC located in the singel operon ectABCask, DNA sequence determination and analysis, genetic organization, expression in Escherichia coli strain X1-Blue
gene ectC, DNA and amino acid sequence determination and analysis, genetic mapping and organization, functional expression in Escherichia coli, the recombinant enzyme expression is osmoregulated in response to medium salinity in Escherichia coli
gene ectC, DNA and amino acid sequence determination and analysis, phylogenetic analysis and genetic organization
gene ectC, encoded in the ectABC gene cluster, sequence determination and analysis, phylogenetic analysis, DNA sequence comparison, expression in Escherichia coli
gene ectC, recombinant expression of a codon-optimized version of C-terminall Strep II-tagged enzyme in Escherichia coli strain BL21 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
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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
-
the ectABC gene cluster is expressed in Escherichia coli M15 (pREP4) by vector pQE30
gene ectC, DNA and amino acid sequence determination and analysis, phylogenetic analysis and genetic organization
gene ectC, DNA and amino acid sequence determination and analysis, phylogenetic analysis and genetic organization
gene ectC, DNA and amino acid sequence determination and analysis, phylogenetic analysis and genetic organization
gene ectC, DNA and amino acid sequence determination and analysis, phylogenetic analysis and genetic organization
gene ectC, DNA and amino acid sequence determination and analysis, phylogenetic analysis and genetic organization
gene ectC, DNA and amino acid sequence determination and analysis, phylogenetic analysis and genetic organization
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
industry
biotechnology
inducible recombinant enzyme expression in Escherichia coli confers the capability to grow on high concentration of osmolytes by increasing the osmotolerance via L-ectoine production
biotechnology
ectoine has importance in dermopharmacy as anti ageing agents in skin creams, as components of shampoo, for oral care and as adjuvants for vaccines
biotechnology
-
ectoine has importance in dermopharmacy as anti ageing agents in skin creams, as components of shampoo, for oral care and as adjuvants for vaccines
-
industry
the engineered Escherichia coli strain has potential industrial application since it produces ectoine at high rates and can avoid the complex down streaming process associated with the conventional bioprocess
industry
-
the engineered Escherichia coli strain has potential industrial application since it produces ectoine at high rates and can avoid the complex down streaming process associated with the conventional bioprocess
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Peters, P.; Galinski, E.A.; Trüper, H.G.
The biosynthesis of ectoine
FEMS Microbiol. Lett.
71
157-162
1990
Halomonas elongata, Halorhodospira halochloris
-
brenda
Ono, H.; Sawada, K.; Khunajakr, N.; Tao, T.; Yamamoto, M.; Hiramoto, M.; Shinmyo, A.; Takano, M.; Murooka, Y.
Characterization of biosynthetic enzymes for ectoine as a compatible solute in a moderately halophilic eubacterium, Halomonas elongata
J. Bacteriol.
181
91-99
1999
Halomonas elongata, Halomonas elongata OUT30018
brenda
Kuhlmann, A.U.; Bremer, E.
Osmotically regulated synthesis of the compatible solute ectoine in Bacillus pasteurii and related Bacillus spp.
Appl. Environ. Microbiol.
68
772-783
2002
Bacillus alcalophilus, Chromohalobacter salexigens (Q9ZEU6), 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 (Q9AP33), Sporosarcina pasteurii, Sporosarcina psychrophila, Virgibacillus pantothenticus, Virgibacillus salexigens
brenda
Reshetnikov, A.S.; Khmelenina, V.N.; Trotsenko, Y.A.
Characterization of the ectoine biosynthesis genes of haloalkalotolerant obligate methanotroph 'Methylomicrobium alcaliphilum 20Z'
Arch. Microbiol.
184
286-297
2006
Methylomicrobium alcaliphilum (Q4JQJ3)
brenda
Louis, P.; Galinski, E.A.
Characterization of genes for the biosynthesis of the compatible solute ectoine from Marinococcus halophilus and osmoregulated expression in Escherichia coli
Microbiology
143
1141-1149
1997
Marinococcus halophilus, Marinococcus halophilus (O06061)
brenda
Nakayama, H.; Yoshida, K.; Ono, H.; Murooka, Y.; Shinmyo, A.
Ectoine, the compatible solute of Halomonas elongata, confers hyperosmotic tolerance in cultured tobacco cells
Plant Physiol.
122
1239-1247
2000
Halomonas elongata, Halomonas elongata OUT30018, no activity in Nicotiana tabacum
brenda
Rajan, L.A.; Joseph, T.C.; Thampuran, N.; James, R.; Chinnusamy, V.; Bansal, K.C.
Characterization and phylogenetic analysis of ectoine biosynthesis genes from Bacillus halodurans
Arch. Microbiol.
190
481-487
2008
Bacillus halodurans (A5A5G3), Bacillus halodurans TCJAR021 (A5A5G3)
brenda
Rajan, L.A.; Joseph, T.C.; Thampuran, N.; James, R.; Kumar, K.A.; Viswanathan, C.; Bansal, K.C.
Cloning and heterologous expression of ectoine biosynthesis genes from Bacillus halodurans in Escherichia coli
Biotechnol. Lett.
30
1403-1407
2008
Bacillus halodurans (A5A5G3), Bacillus halodurans TCJAR021 (A5A5G3)
brenda
Witt, E.M.; Davies, N.W.; Galinski, E.A.
Unexpected property of ectoine synthase and its application for synthesis of the engineered compatible solute ADPC
Appl. Microbiol. Biotechnol.
91
113-122
2011
Halomonas elongata, Halomonas elongata DSM 2581
brenda
Reshetnikov, A.S.; Khmelenina, V.N.; Mustakhimov, I.I.; Kalyuzhnaya, M.; Lidstrom, M.; Trotsenko, Y.A.
Diversity and phylogeny of the ectoine biosynthesis genes in aerobic, moderately halophilic methylotrophic bacteria
Extremophiles
15
653-663
2011
Methylarcula marina (D2KPJ4), Methylarcula marina, Methylarcula marina ML1 (D2KPJ4), Methylobacter marinus (B2CKR7), Methylobacter marinus 7C (B2CKR7), Methylobacter marinus 7C, Methylomicrobium alcaliphilum (B2CKS1), Methylomicrobium alcaliphilum ML1 (B2CKS1), Methylomicrobium alcaliphilum ML1, Methylomicrobium kenyense, Methylomicrobium kenyense (Q307N7), Methylomicrobium kenyense AMO1 (Q307N7), Methylophaga alcalica (A9YZY2), Methylophaga alcalica M8 (A9YZY2), Methylophaga alcalica M8, Methylophaga thalassica (A9YZX7), Methylophaga thalassica, Methylophaga thalassica ATCC 33146 (A9YZX7)
brenda
Kobus, S.; Widderich, N.; Hoeppner, A.; Bremer, E.; Smits, S.
Overproduction, crystallization and X-ray diffraction data analysis of ectoine synthase from the cold-adapted marine bacterium Sphingopyxis alaskensis
Acta Crystallogr. Sect. F
71
1027-1032
2015
Sphingopyxis alaskensis (Q1GNW6), Sphingopyxis alaskensis, Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256 (Q1GNW6)
brenda
Widderich, N.; Kobus, S.; Hoeppner, A.; Riclea, R.; Seubert, A.; Dickschat, J.S.; Heider, J.; Smits, S.H.; Bremer, E.
Biochemistry and crystal structure of ectoine synthase a metal-containing member of the cupin superfamily
PLoS ONE
11
e0151285
2016
Sphingopyxis alaskensis (Q1GNW6), Sphingopyxis alaskensis, Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256 (Q1GNW6)
brenda
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