Crystalline aspartate aminotransferase from Pseudomonas striata
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چکیده
منابع مشابه
Aspartate: 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 ...
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Aspartate aminotransferase from Sulfolobus solfataricus (SsAspAT) is an extremely thermophilic and thermostable dimeric enzyme which retains its structure and reaches maximal activity at 100 degrees C. The structural stability of this protein was investigated by coupling isothermally and thermally induced denaturation studies to molecular modeling. Gel filtration analysis indicated that SsAspAT...
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...
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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...
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and plays a key role in carbon and nitrogen metabolism in plants. The enzyme has been shown to be involved in the shuttling of reducing equivalents from the cytoplasm to chloroplasts, mitochondria, glyoxysomes, and peroxisomes via the malate-aspartate shuttle (Wightman and Forest, 1978). Up to five separate isoforms of AAT have been reported in plants, differing both kinetically and in levels a...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1976
ISSN: 0014-5793
DOI: 10.1016/0014-5793(76)80165-2