{'fraction_non_alphanumeric': 0.038857142857142854, 'fraction_numerical': 0.032, 'mean_word_length': 5.125874125874126, '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}}
4-N-Trimethylaminobutyraldehyde Dehydrogenase: Purification and Characterization of an Enzyme from Pseudomonas sp. 13CM

4-N-trimethylaminobutyraldehyde dehydrogenase from Pseudomonas sp. 13CM was purified 14-fold to apparent homogeneity by hydrophobic chromatography on a Phenyl-Toyopearl, and affinity chromatography was done on a 5′-AMP Sepharose4B in the presence of dithiothreitol. The enzyme was found to be a trimer with identical 55 kDa subunits. The isoeletric point was found to be 5.5. The optimum temperature and pH were 40 °C and pH 10.0. The purified enzyme was further characterized with respect to substrate specificity, kinetic parameters, and analog inhibition. The K m values for 4-N-trimethylaminobutyraldehyde, 4-dimethylaminobutyraldehyde, and NAD+ were 7.4, 51, and 125 μM respectively. The enzyme was inhibited by SH reagents, and by heavy metal ions.