The Reaction of Cytoplasmic Aspartate Aminotransferase with Bromopyruvate
نویسندگان
چکیده
منابع مشابه
Affinity labeling of aspartate aminotransferase isozymes by bromopyruvate.
Incubation with bromopyruvate did not cause appreciable inactivation of either supernatant or mitochondrial isozyme of aspartate aminotransferase from pig heart. In the presence of either L-cysteine sulfinate or L-aspartate, however, bromopyruvate rapidly inactivated both isozymes. Bromopyruvate also acted as a keto acid substrate in the conversion of the pyridoxamine form of both enzymes to th...
متن کاملPhotoinactivation of aspartate aminotransferase.
The cofactor pyridoxal 5’-phosphate bound through an aldimine linkage to lysine residues of the enzyme aspartate amiuotransferase is very stable to irradiation with light of 420 nm. The catalytic function of the enzyme exposed to light absorbed by the cofactor remains unaffected, indicating that pyridoxal 5’-phosphate is not an efficient active site photosensitizer for this aminotransferase. Th...
متن کاملAcylation of aspartate aminotransferase.
1. Acetylation of aspartate aminotransferase from pig heart inhibits completely the enzymic activity when the coenzyme is in the amino form (pyridoxamine phosphate) or when the coenzyme has been removed, but not when the coenzyme is in the aldehyde form (pyridoxal phosphate). 2. The group the acylation of which is responsible for the inhibition has been identified with the in-amino group of a l...
متن کاملAspartate: 2-oxoglutarate aminotransferase from trichomonas vaginalis. Identity of aspartate aminotransferase and aromatic amino acid aminotransferase.
Aspartate: 2-oxoglutarate aminotransferase from the anaerobic protozoon Trichomonas vaginalis was purified to homogeneity and characterized. It is a dimeric protein of overall Mr approx. 100000. Only a single isoenzyme was found in T. vaginalis. The overall molecular and catalytic properties have features in common with both the vertebrate cytoplasmic and mitochondrial isoenzymes. The purified ...
متن کاملThe unfolding and refolding of cytoplasmic aspartate aminotransferase from pig heart.
The unfolding of cytoplasmic aspartate aminotransferase from pig heart in solutions of guanidinium chloride (GdnHCl) was studied. Data from protein fluorescence, c.d. and thiol-group reactivity indicated that the enzyme was unfolded in 6 M-GdnHCl. Spectroscopic studies showed that this unfolding was accompanied by dissociation of the pyridoxal 5'-phosphate cofactor. On dilution of the GdnHCl, r...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1974
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)42254-0