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- W2088572868 abstract "Abstract Tryptophanase from Aeromonas liquefaciens has been purified to homogeniety by employing a heat treatment, (NH4)2SO4 fractionations and hydroxyapatite chromatography. The enzyme binds four moles of pyridoxal 5′-phosphate per mole of enzyme, has s02-,w value of 9.78 S and a mol. wt of 216 000. These properties and the general catalytic properties of the enzyme are similar to other tryptophanase molecules. The enzyme requires pyridoxal 5′-phosphate (Km 2.09·10−6 M), NH4+ or K+ for catalytic activity and besides using tryptophan (Km 2.21·10−4 M), the enzyme can also utilize l -serine, l -cysteine and S- methyl- l -cysteine in catalyzing α,β-elimination and β-replacement reactions. Anthranilic acid (Ki 3.0·10−4 M) alanine (Ki 1.31·10−3 M), and phenylalanine (Ki 7.79·10−3 M) are competitive inhibitors of the tryptophanase reaction. Immunochemical studies indicate that the A. liquefaciens enzyme has some common antigenic determinant sites with the tryptophanases from Escherichia coli, Bacillus alvei, a marine vibrio (K-7), Paracolobactrum coliforme, Micrococcus aerogenes, and Sphaerophorus funduliformis. Each tryptophanase studied has a distinct amino acid composition, but as a group they are characterized by a fairly high content (50–56%) of non-polar amino acids and a very similar total basic amino acid content. The A. liquefaciens enzyme has the highest non-polar and lowest acidic amino acid content of the group, and may be expected to have an electrophoretic mobility significantly different from the other molecules." @default.
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- W2088572868 date "1973-08-01" @default.
- W2088572868 modified "2023-10-12" @default.
- W2088572868 title "Tryptophanase from Aeromonas liquefaciens. Purification molecular weight and some chemical, catalytic and immunochemical properties" @default.
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- W2088572868 doi "https://doi.org/10.1016/0005-2744(73)90276-3" @default.
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