Hormonal discrimination among transcription start sites of aspartate aminotransferase.
نویسندگان
چکیده
منابع مشابه
Mitochondrial aspartate aminotransferase-independent function of the catalytic binding sites.
The enzyme mitochondrial aspartate aminotransferase from beef liver is a dimer of identical subunits. The enzymatic activity of the resolved enzyme is restored upon addition of the cofactor pyridoxal 5-phosphate. The binding of 1 molecule of cofactor restores 50% of the original enzymatic activity, whereas the binding of a 2nd molecule of cofactor brings about more than 95% recovery of the cata...
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Alignments of homologous genomic sequences are widely used to identify functional genetic elements and study their evolution. Most studies tacitly equate homology of functional elements with sequence homology. This assumption is violated by the phenomenon of turnover, in which functionally equivalent elements reside at locations that are nonorthologous at the sequence level. Turnover has been d...
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MOTIVATION Identifying bacterial promoters is an important step towards understanding gene regulation. In this paper, we address the problem of predicting the location of promoters and their transcription start sites (TSSs) in Escherichia coli. The accepted method for this problem is to use position weight matrices (PWMs), which define conserved motifs at the sigma-factor binding site. However ...
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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...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1990
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)39584-5