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2.2.1.6: acetolactate synthase

This is an abbreviated version!
For detailed information about acetolactate synthase, go to the full flat file.

Word Map on EC 2.2.1.6

Reaction

2 pyruvate =

2-acetolactate
+
CO2

Synonyms

aceto-hydroxy acid synthase, acetohydroxy acid synthase, acetohydroxy acid synthase I, acetohydroxy acid synthetase, acetohydroxyacid synthase, acetolactate pyruvate-lyase (carboxylating), acetolactate synthase, acetolactate synthetase, acetolactate-synthase, acetolactic synthetase, AHAS, AHAS II, AHAS1, AHAS2, AHAS3, AHASL, AHASS, alpha-acetohydroxy acid synthetase, alpha-acetohydroxyacid synthase, alpha-acetolactate synthase, alpha-acetolactate synthetase, alpha-ALS, ALS, ALS1, ALS1R, ALS2, AlsS, CalS, catabolic acetolactate synthase, EC 4.1.3.18, GST-mALS, GST-wALS, Ilv2, Ilv6, ilvB, ilvB1, ilvB2, ilvG, IlvN, ilvX, Moilv2, Moilv6, More, PF0935, sll1981, synthase, acetolactate, TM_0548, TM_0549, TTHA1213

ECTree

     2 Transferases
         2.2 Transferring aldehyde or ketonic groups
             2.2.1 Transketolases and transaldolases
                2.2.1.6 acetolactate synthase

Crystallization

Crystallization on EC 2.2.1.6 - acetolactate synthase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
free enzyme and in complex with inhibitors, hanging drop vapor diffusion method, using 1 M sodium potassium tartrate, 0.1 M CHES and 0.1-0.2 M lithium sulfate
in complex with inhibitors N-[(4-methylpyrimidin-2-yl)carbamoyl]-2-nitrobenzenesulfonamide and methyl 2-([(4-methylpyrimidin-2-yl)carbamoyl]sulfamoyl)benzoate, to 3.0 A and 2.8 A resolution, respectively. In both complexes, the inhibitors are bound in the tunnel leading to the active site, such that the sole substituent of the heterocyclic ring is buried deepest and oriented towards the thiamine diphosphate. The cofactor is intact and present most likely as the hydroxylethyl intermediate
in complex with penoxsulam, hanging drop vapor diffusion method, using 1.0 M succinic acid, pH 7.0, 0.1 M HEPES, pH 7.0, and 1% (w/v) PEG monomethyl ether 2000
in complex with propoxycarbazone or thiencarbazone methyl, hanging drop vapor diffusion method, using 1.0 M Na/K tartrate, 0.1 M CHES, and 0.19 M (NH4)2SO4. In complex with bispyribac or pyrithiobac, hanging drop vapor diffusion method, using 20% (w/v) PEG 3350 and 0.2 M sodium citrate tribasic dihydrate or 0.2 M potassium citrate tribasic dihydrate
resolution of the diffraction data for herbicide-AHAS complexes varies between 2.2 A for the chlorsulfuron-bound structure to 2.8 A for the chlorimuron ethyl-bound structure, between 2.5 and 2.9 A for other catalytic subunit-herbicide complexes, overview
-
purified enzyme in the presence of thiamine diphosphate and Mg2+, and in a transition state with a 2-lactyl moiety bound to thiamine diphosphate, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement
sitting drop vapor diffusion method, using polyethylene glycol 300 (30%, w/v), CaAc (200 mM), and sodium cacodylate (100 mM, pH 6.5)
purified recombinant wild-type and selenomethionine-labeled isozyme AHAS III in complex with valine, hanging drop vapour diffusion method, room temperature, 0.0036 ml of protein solution containing 10-25 mg/ml protein and 0.5 M MgCl2, is mixed with reservoir solution containing 30-40% PEG 400, 0.4-0.6 M MgCl2, 100 mM Tris-HCl, pH 8.5, tetragonal or orthorhombic crystals, X-ray diffraction structure determination and analysis at 1.75-2.5 A resolution
-
solution NMR studies. The secondary structure of the FAD binding domain of large subunit ilvB is similar to the structure of this domain in the catalytic subunit of yeast AHAS. The regulatory subunit ilvN interacts with ilvBalpha and ilvBbeta domains of the catalytic subunit and not with the ilvBgamma domain. ilvN binds close to the FAD binding site in ilvBbeta and proximal to the intrasubunit ilvBalpha/ilvBbeta domain interface
-
homology modeling of enzyme based on the structure of the yeast enzyme.In the model, the S167 and S506 residues lie near the FAD binding site, while the S539 residue is found near the thiamine diphosphate binding site
-
crystal structure analysis
free enzyme and in complex with inhibitors, hanging drop vapor diffusion method, using 1 M sodium potassium tartrate, 0.1 M CHES and 0.1-0.2 M lithium sulfate
-
in complex with penoxsulam, hanging drop vapor diffusion method, using 1.0 M succinic acid, pH 7.0, 0.1 M HEPES, pH 7.0, and 1% (w/v) PEG monomethyl ether 2000
in complex with pyruvate