Heterodimeric Aminopeptidase A from Bacillus lichenformis NS115

An aminopeptidase A (EC 3.4.11.7) was purified to homogeneity from Bacillus lichenformis NS115 and its enzymatic properties were characterized. The enzyme had an apparent molecular mass of 64 kDa, consisting of heterodimeric 42 kDa and 22 kDa subunits, and is a new enzyme from N-terminal analysis of...

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Published inBioscience, biotechnology, and biochemistry Vol. 61; no. 11; p. 1934
Main Authors OH, Tae-Kwang, PARK, Mi-Ja, LEE, Jung-Kee, KIM, Hyung-Kwoun, NAM, Hee-Sop
Format Journal Article
LanguageEnglish
Published Tokyo Oxford University Press 01.11.1997
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Abstract An aminopeptidase A (EC 3.4.11.7) was purified to homogeneity from Bacillus lichenformis NS115 and its enzymatic properties were characterized. The enzyme had an apparent molecular mass of 64 kDa, consisting of heterodimeric 42 kDa and 22 kDa subunits, and is a new enzyme from N-terminal analysis of heavy and light subunits. The light subunit had no catalytic activity against the substrate and apparent Km values of heavy and whole enzyme were 0.26 and 0.087 mM of γ-glutamyl-p-nitroanilide, respectively.
AbstractList An aminopeptidase A (EC 3.4.11.7) was purified to homogeneity from Bacillus lichenformis NS115 and its enzymatic properties were characterized. The enzyme had an apparent molecular mass of 64 kDa, consisting of heterodimeric 42 kDa and 22 kDa subunits, and is a new enzyme from N-terminal analysis of heavy and light subunits. The light subunit had no catalytic activity against the substrate and apparent Km values of heavy and whole enzyme were 0.26 and 0.087 mM of γ-glutamyl-p-nitroanilide, respectively.
Author NAM, Hee-Sop
PARK, Mi-Ja
KIM, Hyung-Kwoun
OH, Tae-Kwang
LEE, Jung-Kee
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