{'fraction_non_alphanumeric': 0.03562005277044855, 'fraction_numerical': 0.0079155672823219, 'mean_word_length': 5.2727272727272725, '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}}
Metabolism of guanidinosuccinic acid. I. Characterization of a specific amidino hydrolase from Pseudomonas chlororaphis.

Abstract An enzyme purified from Pseudomonas chlororaphis catalyzes the hydrolysis of N-amidino-l-aspartic acid (guanidinosuccinic acid) to l-aspartic acid and urea. Of a number of other guanidine-containing compounds, only N-amidino-l-glutamate is hydrolyzed by the enzyme. Since N-amidino-d-aspartate is not hydrolyzed, the specificity of the enzyme confirms optical rotatory dispersion measurements which relate the configuration of guanidinosuccinic acid isolated from rat and human urine to that of l-aspartate. The enzyme has a molecular weight in the range of 300,000 and is activated by Co++ in a temperature-dependent reaction.