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4.3.2.2: adenylosuccinate lyase

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

Word Map on EC 4.3.2.2

Reaction

(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
=
fumarate
 +
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide

Synonyms

adenylosuccinase, adenylosuccinate lyase, ADL, ADSL, AMPS lyase, ASASE, ASL, Glutamyl-tRNA synthetase regulatory factor, lyase, adenylosuccinate, PurB, succino AMP-lyase, succino-AMP lyase

ECTree

     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.2 Amidine-lyases
                4.3.2.2 adenylosuccinate lyase

Crystallization

Crystallization on EC 4.3.2.2 - adenylosuccinate lyase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 1.4 M sodium/potassium phosphate pH 7.5 and 4% (v/v) glycerol
the crystal structures of wild-type ADL, and mutant-substrate, H171A-ADS, and -product, H171N-AMP-FUM, complexes are determined to 2.0, 1.85, and 2.0 A resolution, respectively
purified wild-type apo-enzyme and enzyme mutant R303C, high throughput screening by sitting drop method, method optimization, mixing of 0.004 ml of protein solution with 0.004 ml of reservoir solution and equilibration against 0.5 ml of reservoir solution, with a precipitant gradient for the native enzyme of 18-28% w/v PEG 6000, 0.1 M Tris, pH 8.0, and 12.5 mM MgCl2 hexahydrate, and for enzyme mutant R303C, a precipitant gradient of 18-28% w/v PEG 8000, 0.1 M Tris, pH 8.5, and 12.5 mM spermine tetrahydrochloride, X-ray diffraction structure determination and analysis at 2.7 A and 2.6 A resolution, respectively
purified enzyme, X-ray diffraction structure determination is not possible
-
purified enzyme, X-ray diffraction structure determination and analysis at 2.16 A resolution
at a resolution of 2.1 A
-
crystal structure is determined to 2.1 resolution. Hanging drop vapor diffusion method at 18°C
in complex with AMP, at 2.5 A resolution, and modeling of oxalate in the active site. Comparisons with the enzyme from Escherichia coli and with human PurB show close similarity of the active sites, but differences in the way that the subunits are assembled into dimers
at a resolution of 1.8 A