Unknown

Dataset Information

0

Pyridoxal arsenate as a prosthetic group for aspartate aminotransferase.

ABSTRACT: The apoenzyme of aspartate aminotransferase formed a stable, active holoenzyme on treatment with pyridoxal in the presence of arsenate.

SUBMITTER: Ali BR 

PROVIDER: S-EPMC1132644 | biostudies-other | 1992 Jun

REPOSITORIES: biostudies-other

Json Xml

Similar Datasets

Unknown Light-enhanced catalysis by pyridoxal phosphate-dependent aspartate aminotransferase.
| S-EPMC3021986 | biostudies-literature
Unknown Direct evidence that an extended hydrogen-bonding network influences activation of pyridoxal 5'-phosphate in aspartate aminotransferase.
| S-EPMC5392587 | biostudies-literature
Unknown Aspartate aminotransferase Rv3722c governs aspartate-dependent nitrogen metabolism in Mycobacterium tuberculosis.
| S-EPMC7181641 | biostudies-literature
Unknown Expression, purification, crystallization, data collection and preliminary biochemical characterization of methicillin-resistant Staphylococcus aureus Sar2028, an aspartate/tyrosine/phenylalanine pyridoxal-5'-phosphate-dependent aminotransferase.
| S-EPMC2335000 | biostudies-literature
Unknown Methionine regeneration and aspartate aminotransferase in parasitic protozoa.
| S-EPMC95336 | biostudies-literature
Unknown Aspartate: 2-oxoglutarate aminotransferase from trichomonas vaginalis. Identity of aspartate aminotransferase and aromatic amino acid aminotransferase.
| S-EPMC1152940 | biostudies-other
Unknown Acylation of aspartate aminotransferase.
| S-EPMC1271239 | biostudies-other
Unknown Studies on the changes in protein fluorescence and enzymic activity of aspartate aminotransferase on binding of pyridoxal 5'-phosphate.
| S-EPMC1168433 | biostudies-other
Unknown Biochemical and structural characterization of mouse mitochondrial aspartate aminotransferase, a newly identified kynurenine aminotransferase-IV.
| S-EPMC3046307 | biostudies-literature
Unknown Ground-state electronic destabilization via hyperconjugation in aspartate aminotransferase.
| S-EPMC3425665 | biostudies-literature