A pyridoxal-phosphate protein. The enzyme cleaves a carbon-sulfur bond, releasing hydrogen sulfide and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form 2-oxobutanoate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase
Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
A pyridoxal-phosphate protein. The enzyme cleaves a carbon-sulfur bond, releasing hydrogen sulfide and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form 2-oxobutanoate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase
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
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
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
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
the enzyme displays a strong affinity to homocysteine, followed by methionine and cysteine when compared with non-S amino acids, confirming its potency against homocysteinuria related diseases, and as an anti-cardiovascular agent and a specific biosensor for homocysteinuria
the enzyme displays a strong affinity to homocysteine, followed by methionine and cysteine when compared with non-S amino acids, confirming its potency against homocysteinuria related diseases, and as an anti-cardiovascular agent and a specific biosensor for homocysteinuria
Homocysteine desulphurase activity in trichomonads
IRCS Med. Sci. Libr. Compend.
13
493-494
1985
no activity in Crithidia fasciculata, no activity in Escherichia coli, no activity in Entamoeba histolytica, no activity in Herpetomonas muscarum, no activity in Leishmania mexicana mexicana, no activity in Leishmania tarentolae, no activity in mouse, no activity in Tetrahymena pyriformis, no activity in Trichomonas foetus, Trichomonas batrachorum, Trichomonas vaginalis