Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:6.1.1.12 (aspartyl-tRNA synthetase)
 233 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Several lines of evidence establish that the crystallizable aspartyl-tRNA synthetase from Baker's yeast contains some covalently bound glucose: (i) a positive staining of the enzyme was obtained after polyacrylamide gel electrophoresis followed by the concanavalin A-peroxidase test which is specific for glucose and mannose containing proteins; (ii) thin-layer chromatography and gas-liquid chromatography revealed the presence of glucose in enzyme hydrolysates; (iii) immunoaffinoelectrophoresis in agarose gels containing concanavalin A and antibodies raised against aspartyl-tRNA synthetase showed that the enzyme was able to precipitate entirely in the lectin. Finally incubation of the enzyme with [14C]glucose or [14C]glucose 6-phosphate led to the incorporation of radioactivity into trichloroacetic acid-precipitable protein. Indeed immunoprecipitation of [14C]glucose-labelled aspartyl-tRNA synthetase with specific antibodies using the rocket method followed by autoradiography gave a radioactive peak. This last result also demonstrates the possibility of in vitro glycosylation of yeast aspartyl-tRNA synthetase.
 ...
PMID:Glycosylation of yeast aspartyl-tRNA synthetase. Affinity labelling by glucose and glucose 6-phosphate. 635 53

The usefulness of X-ray data derived from space-grown protein crystals for calculating a more accurate structure is reviewed here for three model proteins. These include the plant sweetening protein, thaumatin, from Thaumatococcus daniellii; the aspartyl-tRNA synthetase from Thermus thermophilus; and pea lectin from Pisum sativum. In all three cases, X-ray diffraction data collected from protein crystals obtained under reduced gravity lead to better defined initial electron density maps, facilitating model building and improved crystallographic statistics. With thaumatin, the phasing power of the anomalous scattering atom, sulfur, is used to determine protein crystal quality in terms of its usefulness for ab initio structure determination. Thaumatin crystals grown under microgravity provided improved phasing statistics compared to those of Earth-grown crystals. Consequently, generating a de novo protein model of higher quality was facilitated using X-ray diffraction data from space-grown crystals. This lends evidence to the possibility that a microgravity environment can favor protein crystal growth and, subsequently, be more useful for structure determination.
 ...
PMID:Space-grown protein crystals are more useful for structure determination. 1244 51