Open Access@KRIBBDivision of A.I. & Biomedical ResearchMetabolic Regulation Research Center1. Journal Articles
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.
- ISSN
- 0916-8451
- Publisher
- T&F (Taylor & Francis)
- Full Text Link
- http://dx.doi.org/10.1271/bbb.61.1934
- Type
- Article
- Appears in Collections:
- Division of A.I. & Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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