Literature summary for 4.2.1.108 extracted from

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 (2015), Acta Crystallogr. Sect. F, 71, 1027-1032 .

Search for more literature for 4.2.1.108

Cloned(Commentary)

Cloned (Comment)	Organism
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	Sphingopyxis alaskensis

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Sphingopyxis alaskensis

Crystallization (Comment)

Organism

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

Sphingopyxis alaskensis

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
32700	-	recombinant Strep II-tagged enzyme, gel filtration	Sphingopyxis alaskensis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
(2S)-4-acetamido-2-aminobutanoate	Sphingopyxis alaskensis	-	L-ectoine + H2O	-	?
(2S)-4-acetamido-2-aminobutanoate	Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256	-	L-ectoine + H2O	-	?

Organism

Organism	UniProt	Comment	Textmining
Sphingopyxis alaskensis	Q1GNW6	i.e. Sphingomonas alaskensis	-
Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256	Q1GNW6	i.e. Sphingomonas alaskensis	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant C-terminall Strep II-tagged enzyme from Escherichia coli by affinity chromatography and gel filtration to homogeneity	Sphingopyxis alaskensis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(2S)-4-acetamido-2-aminobutanoate	-	Sphingopyxis alaskensis	L-ectoine + H2O	-	?
(2S)-4-acetamido-2-aminobutanoate	-	Sphingopyxis alaskensis DSM 13593 / LMG 18877 / RB2256	L-ectoine + H2O	-	?

Subunits

Subunits	Comment	Organism
dimer	-	Sphingopyxis alaskensis

Synonyms

Synonyms	Comment	Organism
EctC	-	Sphingopyxis alaskensis
L-ectoine synthase	UniProt	Sphingopyxis alaskensis
SaEctC	-	Sphingopyxis alaskensis

General Information

General Information	Comment	Organism
evolution	ectoine biosynthetic genes (ectABC) are widely distributed in bacteria, ectoine synthase is a member of the cupin superfamily	Sphingopyxis alaskensis
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	Sphingopyxis alaskensis