4.4.1.2: homocysteine desulfhydrase
This is an abbreviated version!
For detailed information about homocysteine desulfhydrase, go to the full flat file.
Reaction
Synonyms
desulfhydrase, homocysteine, homocysteine desulfurase, Hyc gamma-lyase
ECTree
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Engineering
Engineering on EC 4.4.1.2 - homocysteine desulfhydrase
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induction of the enzyme is mainly sulfur amino-acid-dependent, especially methionine and homocysteine. The induction of the enzyme in response to various amino acids is evaluated, and the results reveal that sulfur-containing amino acids strongly induce Hcy gamma-lyase production by the isolate when compared with other amino acids. The maximum enzyme productivity is detected in the presence of methionine (1.8 U/mg), homocysteine (1.2 U/mg), cysteine (1.23 U/mg), and asparagine (1.2 U/mg). Some enzyme activity is also detected when using various non-sulfur amino acids as substrates, such as glutamine, alanine, and phenylalanine, indicating the multifunctional deaminating catalytic activity of the crude enzyme. The lowest enzyme activity is detected in the presence of tyrosine and lysine
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the influence of different carbon sources (0.05-0.2%) on the enzyme is assessed when using 100 mM L-methionine as the substrate. From the data, the highest enzyme yield is obtained with 0.15% sucrose (2.54 U/mg), followed by glucose (2.18 U/mg), representing about 1.42- and 1.2-fold increments, respectively, over the control (1.8 U/mg). The enzyme productivity increases about 12.7fold when using 0.15% sucrose over a carbon-free medium
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induction of the enzyme is mainly sulfur amino-acid-dependent, especially methionine and homocysteine. The induction of the enzyme in response to various amino acids is evaluated, and the results reveal that sulfur-containing amino acids strongly induce Hcy gamma-lyase production by the isolate when compared with other amino acids. The maximum enzyme productivity is detected in the presence of methionine (1.8 U/mg), homocysteine (1.2 U/mg), cysteine (1.23 U/mg), and asparagine (1.2 U/mg). Some enzyme activity is also detected when using various non-sulfur amino acids as substrates, such as glutamine, alanine, and phenylalanine, indicating the multifunctional deaminating catalytic activity of the crude enzyme. The lowest enzyme activity is detected in the presence of tyrosine and lysine
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up
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the influence of different carbon sources (0.05-0.2%) on the enzyme is assessed when using 100 mM L-methionine as the substrate. From the data, the highest enzyme yield is obtained with 0.15% sucrose (2.54 U/mg), followed by glucose (2.18 U/mg), representing about 1.42- and 1.2-fold increments, respectively, over the control (1.8 U/mg). The enzyme productivity increases about 12.7fold when using 0.15% sucrose over a carbon-free medium
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