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4.3.2.1: argininosuccinate lyase

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

Word Map on EC 4.3.2.1

Reaction

2-(Nomega-L-arginino)succinate
=
fumarate
 +
L-arginine

Synonyms

AL, ARG4, ArgH, arginine-succinate lyase, argininosuccinase, Argininosuccinate lyase, argininosuccinic acid lyase, Arginosuccinase, ASAL, ASL, delta2 crystallin, delta2-crystallin, hASL, L-argininosuccinate arginine-lyase, lyase, argininosuccinate, Rv1659

ECTree

     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.2 Amidine-lyases
                4.3.2.1 argininosuccinate lyase

Crystallization

Crystallization on EC 4.3.2.1 - argininosuccinate lyase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
S283A mutant, hanging-drop vapor diffusion at room temperatur, 9 mg/ml protein in 10 mM Tris-HCl, pH 7.5 and 1 mM EDTA is preincubated with 75 mM argininosuccinate, subsequently 0.005 ml drops of the solution are mixed with an equal ammount of precipitating solution consisting of 12% polyethylene glycol 2000 MME, 300 mM MgCl2, 100 mM HEPES, pH 7.4, crystals diffract to 1.96 A resolution
-
apoenzyme and complex of double loop mutant with sulfate, growing at room temperature using the hanging drop vapor diffusion method, molecular replacement at 2.2 A resolution for the DLM-sulfate complex, 2.5 A resolution for the apoenzyme
-
crystallized from a highly concentrated sample of purified recombinant alpha-methylacyl-CoA-racemase with arginosuccinate lyase as a minor impurity, growing at room temperature in mother liquid consisting of 1.26 M ammonium phosphate pH 7.0, small bipyramidal crystals, molecular replacement at 2.44 A resolution
-
hanging-drop vapor diffusion, crystal structure of Q286R mutant at 2.65 A
-
purified recombinant His-tagged enzyme, microbatch-under-oil method, mixing of 0.002 ml of 9.5 mg/ml protein in 25 mM phosphate buffer, pH 7.4, with 0.002 ml of precipitant solution containing 100 mM Bis-Tris, pH 5.5, 25% w/v polyethylene glycol 3350, X-ray diffraction structure determination and analysis at 2.40 A resolution, molecular replacement method
to 2.5 A resolution, space group R3