Heterodimeric aminopeptidase a from Bacillus licheniformis NS115

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Title
Heterodimeric aminopeptidase a from Bacillus licheniformis NS115
Author(s)
Tae Kwang Oh; Mi-Ja Park; Jung Kee Lee; Hyung Kwoun Kim; Hee-Sop Nam
Bibliographic Citation
Bioscience Biotechnology and Biochemistry, vol. 61, no. 11, pp. 1934-1936
Publication Year
1997
Abstract
An aminopeptidase A (EC 3.4.11.7) was purified to homogeneity from Bacillus licheniformis 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.
Keyword
Bacillus licheniformisaminopeptidase Aheterodimer
ISSN
0916-8451
Publisher
T&F (Taylor & Francis)
DOI
http://dx.doi.org/10.1271/bbb.61.1934
Type
Article
Appears in Collections:
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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