{'fraction_non_alphanumeric': 0.04470359572400389, 'fraction_numerical': 0.015549076773566569, 'mean_word_length': 4.919540229885057, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
2-Aminoadipate-2-oxoglutarate aminotransferase isoenzymes in human liver: a plausible physiological role in lysine and tryptophan metabolism.

Two major 2-aminoadipate aminotransferase (AadAT) activities of human liver extract were separated by DEAE-Sepharose column chromatography. The faster eluting enzyme was designated AadAT-I and the other one AadAT-II. AadAT-I had a hgih Km value for aminoadipate, 20 mmol/l, and a low Km value for glutamate, 1.4 mmol/l. In contrast, AadAT-II had a low Km value for aminoadipate, 0.25 mmol/l, and a high Km value for glutamate, 12.5 mmol/l. AadAT-I and AadAT-II were mainly localized in the supernatant and mitochondrial fraction, respectively. AadAT-I demonstrated only glutamate-2-oxoadipate or 2-aminoadipate-2-oxoglutarate aminotransferase activities. AadAT-II further showed the activity of tryptophan and kynurenine. On the basis of Km values and subcellular localization of the isoenzymes, a plausible role was suggested for them involving the metabolism of lysine and tryptophan.