Arginine deiminase from Halobacterium salinarium. Purification and properties.
Arginine deiminase from the extreme halophilic archaebacterium Halobacterium salinarium was purified to homogeneity in a four-step procedure with a 310-fold enrichment. The enzyme consists of two identical subunits of 55 kDa; its native molecular mass is 105 kDa. The pI of 4.7 indicates that acidic nature of the protein, which is evidenced by its amino acid composition, which shows an excess of more than 15% of acidic amino acids. The N-terminal amino acid of the enzyme is lysine. Arginine deiminase from Halobacterium salinarium exhibits its highest catalytic activity in the presence of 3.5 M-NaCl, pH 7.6, and at 40 degrees C. The half-activity constant, Ks, for arginine is 3.1 mM. The enzyme is inhibited by ornithine.
Monstadt
G M
GM
Institut für Physiologische Chemie, Ruhr-Universität Bochum, Germany.
Holldorf
A W
AW
D000596:Amino Acids / Q000032:analysis; D002845:Chromatography; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D017886:Durapatite; D004591:Electrophoresis, Polyacrylamide Gel; D006217:Halobacterium / Q000201:enzymology* / Q000254:growth & development; D006867:Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D006882:Hydroxyapatites; D007525:Isoelectric Focusing; D007700:Kinetics; D008970:Molecular Weight
D000596:Amino Acids; D006882:Hydroxyapatites; D017886:Durapatite; D006867:Hydrolases; C019723:arginine deiminase