Any feedback?
Information on EC 4.2.1.108 - ectoine synthase
for references in articles please use BRENDA:EC4.2.1.108Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Word Map
- 4.2.1.108
-
halophil
-
diaminobutyric
- halomonas
- elongata
-
hydroxyectoine
-
osmoprotectant
-
ectabc
-
methanotrophs
-
halotolerant
-
l-2,4-diaminobutyric
- salexigens
-
methylomicrobium
-
osmoadaptation
- biotechnology
- industry
The enzyme appears in viruses and cellular organisms
Synonyms
ectoine synthase, l-ectoine synthase, saectc, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(Sa)Ect
EctC
ectoine synthase
L-ectoine synthase
SaEctC
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(2S)-4-acetamido-2-aminobutanoate = L-ectoine + H2O
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
condensation
condensation
Halalkalibacterium halodurans TCJAR021
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
130457-09-9
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
?
(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
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
Halalkalibacterium halodurans
-
-
-
?
N4-acetyl-L-2,4-diaminobutyrate
2-methyl-1,4,5,6-tetrahydropyrimidine-4-carboxylic acid + H2O
Halalkalibacterium halodurans TCJAR021
-
-
-
?
N4-acetyl-L-2,4-diaminobutyrate
L-ectoine + H2O
Halalkalibacterium halodurans
-
-
-
?
N4-acetyl-L-2,4-diaminobutyrate
L-ectoine + H2O
Halalkalibacterium halodurans TCJAR021
-
-
-
?
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
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
?
(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
Halalkalibacterium halodurans
-
-
-
?
N4-acetyl-L-2,4-diaminobutyrate
2-methyl-1,4,5,6-tetrahydropyrimidine-4-carboxylic acid + H2O
Halalkalibacterium halodurans TCJAR021
-
-
-
?
N4-acetyl-L-2,4-diaminobutyrate
L-ectoine + H2O
Halalkalibacterium halodurans
-
-
-
?
N4-acetyl-L-2,4-diaminobutyrate
L-ectoine + H2O
Halalkalibacterium halodurans TCJAR021
-
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
additional information
additional information
Michaelis-Menten-kinetics
-
additional information
additional information
-
Michaelis-Menten-kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15
20
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 30
-
the temperature optimum shifts from 0°C to 30°C with increasing NaCl concentration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
formerly Halomonas elongata, strain DSM 3043, gene ectC encoded in the ectABC gene cluster
SwissProt
brenda
Halalkalibacterium halodurans
Halalkalibacterium halodurans TCJAR021
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
Halalkalibacterium halodurans
the ectABC gene cluster expressed in Escherichia coli M15 (pREP4)
TrEMBL
brenda
Halalkalibacterium halodurans TCJAR021
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
MH020164
phylogenetic analysis of nucleotides and amino acids reveals that the ectA, B and C sequences of Bacillus clausii NIOT-DSB04 were conserved in many eubacteria
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
-
evolution
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256
-
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
Alkalihalobacillus clausii NIOT-DSB04
-
phylogenetic analysis of nucleotides and amino acids reveals that the ectA, B and C sequences of Bacillus clausii NIOT-DSB04 were conserved in many eubacteria
-
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
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
MH020164
the enzyme is involved in ectoine biosynthesis. Ectoine is a compatible solute, serves as a protective compound in many halophilic eubacterial cells under stress
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)
-
metabolism
Alkalihalobacillus clausii NIOT-DSB04
-
the enzyme is involved in ectoine biosynthesis. Ectoine is a compatible solute, serves as a protective compound in many halophilic eubacterial cells under stress
-
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
-
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
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
-
physiological function
-
extraordinary protective properties of 5-amino-3,4-dihydro-2H-pyrrole-2-carboxylate produced by ectoine synthase
-
Show AA Sequence and Transmembrane Helices (5457 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned into the expression vector pQE30 with a 6His-tag and expressed in Escherichia coli JM109 M15 cells
MH020164
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
-
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
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
strain TCJAR021, expression in Escherichia coli M15 (pREP4)
Halalkalibacterium halodurans
the ectABC gene cluster is expressed in Escherichia coli M15 (pREP4) by vector pQE30
Halalkalibacterium halodurans
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Halalkalibacterium halodurans
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
Halalkalibacterium halodurans TCJAR021
-
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
Halalkalibacterium halodurans
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
Halalkalibacterium halodurans TCJAR021
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Peters, P.; Galinski, E.A.; Trper, H.G.
The biosynthesis of ectoine
FEMS Microbiol. Lett.
71
157-162
1990
Halorhodospira halochloris, Halomonas elongata
-
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
Alkalihalobacillus alcalophilus, Virgibacillus pantothenticus, Sporosarcina psychrophila, no activity in Bacillus cereus, no activity in Bacillus circulans, no activity in Bacillus licheniformis, no activity in Bacillus megaterium, no activity in Bacillus subtilis, Virgibacillus salexigens, no activity in Bacillus thuringiensis, no activity in Aneurinibacillus aneurinilyticus, no activity in Paenibacillus polymyxa, Sporosarcina pasteurii (Q9AP33), Sporosarcina pasteurii, Chromohalobacter salexigens (Q9ZEU6), no activity in Bacillus cereus DSM 31, no activity in Aneurinibacillus aneurinilyticus DSM 5562, no activity in Bacillus subtilis JH642
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
Methylotuvimicrobium 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 (O06061), Marinococcus halophilus
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, no activity in Nicotiana tabacum, Halomonas elongata OUT30018
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
Halalkalibacterium halodurans (A5A5G3), Halalkalibacterium 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
Halalkalibacterium halodurans (A5A5G3), Halalkalibacterium 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
Methylophaga thalassica (A9YZX7), Methylophaga thalassica, Methylophaga alcalica (A9YZY2), Methylobacter marinus (B2CKR7), Methylotuvimicrobium alcaliphilum (B2CKS1), Methylarcula marina (D2KPJ4), Methylarcula marina, Methylotuvimicrobium kenyense (Q307N7), Methylotuvimicrobium kenyense, Methylotuvimicrobium alcaliphilum ML1 (B2CKS1), Methylobacter marinus 7C (B2CKR7), Methylobacter marinus 7C, Methylophaga thalassica ATCC 33146 (A9YZX7), Methylophaga alcalica M8 (A9YZY2), Methylophaga alcalica M8, Methylotuvimicrobium kenyense AMO1 (Q307N7), Methylarcula marina ML1 (D2KPJ4)
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
Anburajan, L.; Meena, B.; Vinithkumar, N.; Kirubagaran, R.; Dharani, G.
Functional characterization of a major compatible solute in Deep Sea halophilic eubacteria of active volcanic Barren Island, Andaman and Nicobar Islands, India
Infect. Genet. Evol.
73
261-265
2019
Alkalihalobacillus clausii (MH020164), Alkalihalobacillus clausii, Alkalihalobacillus clausii NIOT-DSB04 (MH020164)
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 4.2.1.108)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
