Structures of aspartate aminotransferases fromTrypanosoma brucei,Leishmania majorandGiardia lamblia
نویسندگان
چکیده
منابع مشابه
Primary structures of aspartate aminotransferases.
three residues seems to be common to all the serine enzymes and has become known as the ‘charge-relay system’. Its function is to transfer a negative (or partial negative) charge from the aspartic acid residue to the oxygen atom of the hydroxy group of serine. This obviously increases the nucleophilicity of the serine, but the important point is that the charge is developed in the absence of bu...
متن کاملSelective permeability of rat liver mitochondria to purified aspartate aminotransferases in vitro.
1. A method was devised to allow determination of intramitochondrial aspartate amino-transferase activity in suspensions of intact mitochondria. 2. Addition of purified rat liver mitochondrial aspartate aminotransferase to suspensions of rat liver mitochondria caused an apparent increase in the intramitochondrial enzyme activity. No increase was observed when the mitochondria were preincubated ...
متن کاملPartial purification and characterization of aspartate aminotransferases from seedling oat leaves.
As relatively little information is available on the properties of aspartate aminotransferase from photosynthetic tissue, isolation and characterization of the two major electrophoretically distinct forms of this enzyme from seedling oat leaf homogenates were undertaken. These two forms are designated I for the more anionic form and II for the less anionic form. Form I, 80 to 90% of the total a...
متن کاملEffects of temperature on the steady-state kinetics and measurement of aspartate aminotransferases.
We examined the effects of temperature on the activity and steady-state kinetics of aspartate aminotransferase (EC 2.6.1.1), using purified human soluble (s-AspAT) and mitochondrial (m-AspAT) isoenzymes, human serum, and porcine s-AspAT. All enzymes obeyed similar linear Arrhenius relationships over the range 20-40 degrees C. Apparent energies of activation (52.3 kJ.mol-1) and ratios of activit...
متن کاملPhylobiochemical characterization of class-Ib aspartate/prephenate aminotransferases reveals evolution of the plant arogenate phenylalanine pathway.
The aromatic amino acid Phe is required for protein synthesis and serves as the precursor of abundant phenylpropanoid plant natural products. While Phe is synthesized from prephenate exclusively via a phenylpyruvate intermediate in model microbes, the alternative pathway via arogenate is predominant in plant Phe biosynthesis. However, the molecular and biochemical evolution of the plant arogena...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section F Structural Biology Communications
سال: 2015
ISSN: 2053-230X
DOI: 10.1107/s2053230x15001831