EC Number   |
Protein Variants |
Reference |
|---|
    2.4.2.7 | M136T |
10.3% loss of activity |
659576 |
| 2.4.2.7 | more |
a naturally occuring mutation T596G leading to amino acid exchange F199C in hypoxanthine guanine phosphoribosyltransferase, HPRT, EC 2.4.2.8, with 92% reduced activity and a severe gouty arthritis phenotype, while the mutation or HPRT deficiency typically lead to a 2-3fold increased APRT activity in erythrocytes. Modeling of the mutated protein for prediction of the mechanisms of partial enzymatic activity |
701979 |
| 2.4.2.7 | more |
alignment of amino acid sequences, correlation between human clinical missense mutations and structure, structure taken from Leishmania donovani enzyme |
638166 |
| 2.4.2.7 | more |
antisense expression of the enzyme for opression of the APT2 gene in Arabidopsis thaliana leads to lower AMP content, lower pollen germination rates, and some abnormalities in leaf phenotypes and flowering timing in the transgenic plants, overview |
676537 |
| 2.4.2.7 | more |
construction of an aprth knockout strain (Tt27DELTAAPRTh) and an aprth-overexpressing strain (Tt27NStHisAPRTh) of Thermus thermophilus in minimal medium. The Tt27DELTAAPRTh strain exhibits delayed growth and requires approximately 36 h to reach the early stationary phase, whereas the wild-type strain reached this phase after 21 h of cultivation. The Tt27NStHisAPRTh strain exhibits better growth than even the wild-type strain |
-, 759432 |
| 2.4.2.7 | more |
covalent immobilization of TtAPRT2 through surface exposed Lys residues promotes a multipoint covalent attachment which leads to higher degree of rigidification, thereby increasing the thermal stability of the protein. Dimeric TtAPRT2 is immobilized onto glutaraldehyde-activated magnetic iron oxide porous microparticles by two different strategies: (a) an enzyme immobilization at pH 8.5 to encourage the immobilization process by N-termini (MTtAPRT2A, MTtAPRT2B, MTtAPRT2C) or (b) an enzyme immobilization at pH 10.0 to encourage the immobilization process through surface exposed lysine residues (MTtAPRT2D, MTtAPRT2E, MTtAPRT2F). According to catalyst load experiments, MTtAPRT2B (activity: 480 IU/g biocatalyst, activity recovery 52%) and MTtAPRT2F (activity 507 IU/g biocatalyst, activity recovery 44%) are chosen as optimal derivatives. The potential reusability of MTtAPRT2B and MTtAPRT2F is also tested. Finally, MTtAPRT2F is employed in the synthesis of nucleoside-5'-monophosphate analogues. 0.025 ml of the bead suspension (0.020 mg/ml) are washed and equilibrated in corresponding binding buffer containing 50 mM potassium phosphate buffer, pH 8.5, 50 mM sodium borate buffer, pH 10.0, or 50 mM sodium borate buffer, pH 10.6, during 4 h at 25°C |
-, 758925 |
| 2.4.2.7 | more |
determination and phenotype analysis of a naturally occuring mutation in the APRT gene by a homozygous 254 bp deletion-8 bp insertion mutation in exon 3, the patients shows sever renal failure, with pathological presence of adenine in both biological fluids, urinary stone excretion, and no enzyme activityin the hemolysate, overview |
673115 |
| 2.4.2.7 | more |
heterozygotes for the 254 bp deletion-8 bp insertion of the APRT gene show a 69% lower APRT enzymatic activity |
673115 |
| 2.4.2.7 | more |
identification of three cases of APRT*Q0 /APRT*J compound heterozygote-type APRT deficiency, genotyping, overview |
706077 |
| 2.4.2.7 | D99N |
mutant enzyme has very low activity |
-, 724940 |
