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2.6.1.1: aspartate transaminase

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

Word Map on EC 2.6.1.1

Reaction

L-aspartate
+
2-oxoglutarate
=
oxaloacetate
 +
L-glutamate

Synonyms

2-oxoglutarate-glutamate aminotransferase, AAT, AAT-2, AAT-3, AAT3, aatA, AATase, aatB3, all2340, alr1039, alr2765, alr4853, aminotransferase, aspartate, aoa/coa, AsAT, Asp AT, aspartate alpha-ketoglutarate transaminase, aspartate aminotransferase, aspartate aminotransferase 1, aspartate aminotransferase A, aspartate AT, aspartate transaminase, aspartate, 2-oxoglutarate aminotransferase, aspartate-2-oxoglutarate transaminase, aspartate/(R)-cysteate:2-oxoglutarate aminotransferase, aspartate/tyrosine/phenylalanine pyridoxal-5'-phosphate-dependent aminotransferase, aspartate:2-oxoglutarate amino-transferase, aspartate:2-oxoglutarate aminotransferase, aspartic acid aminotransferase, aspartic aminotransferase, aspartyl aminotransferase, AspAT, AspATSs, aspB, aspC, AspT, AST, AST-Bb, AtPAT, bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase, C-S lyase, CAA1, cAST, Cgl0240, class Ibeta AAT, EcAspAT, GL50803_91056, glutamate oxaloacetate transaminase, glutamate oxaloacetate transaminase 1, glutamate-oxalacetate aminotransferase, glutamate-oxalate transaminase, glutamate-oxaloacetate transaminase 1, glutamic oxalic transaminase, glutamic oxaloacetic transaminase, glutamic-aspartic aminotransferase, glutamic-aspartic transaminase, glutamic-oxalacetic transaminase, glutamic-oxaloacetic transaminase, GOT, GOT (enzyme), GOT1, GOT1L1, GOT2, KAT IV, L-aspartate aminotransferase, L-aspartate transaminase, L-aspartate-2-ketoglutarate aminotransferase, L-aspartate-2-oxoglutarate aminotransferase, L-aspartate-2-oxoglutarate-transaminase, L-aspartate-alpha-ketoglutarate transaminase, L-aspartate:2-oxoglutarate aminotransferase, L-aspartateartate aminotransferase, L-aspartic aminotransferase, L-AspAT, mitAAT, More, oxaloacetate transferase, oxaloacetate-aspartate aminotransferase, Pat, PfAspAT, plastid aspartate aminotransferase, prephenate aminotransferase, protein TT0402, PT-AAT, Rv3722c, Sar2028, SsAspAT, Tb11.02.2740, transaminase A

ECTree

     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.1 aspartate transaminase

Renatured

Renatured on EC 2.6.1.1 - aspartate transaminase

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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
at 7 M urea and 25°C
guanidinium hydrochloride denatured premature form pmAspAT cannot refold at 30°C, but refolds rapidly in presence of the intramitochondrial chaperone homologues GroEL and GroES
-
in the presence of 0.01 mM pyridoxal 5'-phosphate
-
reconstitution of holoenzyme after purification of apoenzyme with pyridoxal 5'-phosphate
-
reconstitution of holoenzyme after purification of apoenzyme with the inhibitor N-5'-phosphopyridoxyl L-aspartate
-
reconstitution of holoenzyme with pyridoxal 5'-phosphate or pyridoxamine 5'-phosphate
refolding of SsAspAT can be accelerated by increasing the temperature from 25 to 50°C. Although refolding is faster at 50°C (35% of native enzyme) the highest yield of renaturation is obtained at 37°C (70% reactivation), similar to the yield of 65% of initial activity that is obtained at 25°C
reversible dissociation and unfolding of the dimeric enzyme by guanidine hydrochloride
-
thermal denaturation is not reversible
-
unfolding in 6 M guanidine hydrochloride for different periods of time. Reactivation of equilibrium-unfolded mAAT is sigmoidal, reactivation of the short term unfolded protein displays a double exponential behavior consistent with the presence of fast and slow refolding species. The presence of coenzyme does not perturb the kinetics or pathway of refolding. Covalently attached PLP slows down the interconversion between fast and slow folding populations of unfolded states. Additional structural rearrangements occurring both in the unfolded state and in populations of folding intermediates along the folding pathway
-
wild-type and mutants, unfolding by guanidinium hydrochloride and renaturing kinetics, fluorescent spectrometric analysis