Open AccessHeterodimeric Aminopeptidase A fromBacillus licheniformisNS115
Author(s) -
Tae-Kwang Oh,
Mi-Ja Park,
Jung-Kee Lee,
HyungKwoun Kim,
Hee-Sop Nam
Publication year - 1997
Publication title -
bioscience biotechnology and biochemistry
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.61.1934
Subject(s) - bacillus licheniformis , enzyme , aminopeptidase , molecular mass , biochemistry , chemistry , protein subunit , substrate specificity , substrate (aquarium) , bacillus (shape) , biology , bacteria , amino acid , bacillus subtilis , microbiology and biotechnology , gene , leucine , ecology , genetics
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 K(m) values of heavy and whole enzyme were 0.26 and 0.087 mM of gamma-glutamyl-p-nitroanilide, respectively.
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