Aminopeptidase I activities in several microorganisms
Keyword(s):
Aminopeptidase I activity which was found to be localized in the same subcellular fraction and to be similarly heat stable was partially purified by a common procedure from Escherichia coli B, Escherichia coli K12, Enterobacter aerogenes, Salmonella typhimurium, Serratia marcescans, Pseudomonas aeruginosa, and Proteus vulgaris. The enzyme preparations were shown to contain a single aminopeptidase active toward both leucylleucine and methionylalanylserine by mixed-substrate initial-velocity kinetic analysis. The Km value for leucylleucine was virtually identical for the aminopeptidases of all of the organisms, as was the Km value for methionylalanylserine.
2017 ◽
Vol 1
(2)
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pp. 48-60
2020 ◽
Vol 7
(1)
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pp. 8-18
2019 ◽
pp. 1-8
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2020 ◽
Vol 15
(2)
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pp. 48-52