Biomaterial Database

[Physicochemical and enzymatic properties of Aspergillus oryzae aminopeptidase]. 1980

S V Verbilenko, and M V Kolodzeiskaia

The paper deals with properties of Aspergillus oryzae (strain KC) purified aminopeptidase. The enzyme is homogeneous in electrophoresis in polyacrylamide gel and enzyme-electrophoresis with the synthetic substrate leucyl-beta-naphthylamide applied. The molecular mass is 60000-61000 Daltons. The amino acidic composition of the enzyme is characterized by a high content of dicarboxylic acids. The substrate specificity is studied. Leucyl-glycyl-glycin and leucinamide are most intensive in splitting. Peptides with a blocked amino group are not hydrolyzed.

UI	MeSH Term	Description	Entries
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D008970	Molecular Weight	The sum of the weight of all the atoms in a molecule.	Molecular Weights,Weight, Molecular,Weights, Molecular
D000596	Amino Acids	Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.	Amino Acid,Acid, Amino,Acids, Amino
D000626	Aminopeptidases	A subclass of EXOPEPTIDASES that act on the free N terminus end of a polypeptide liberating a single amino acid residue. EC 3.4.11.	Aminopeptidase
D001230	Aspergillus	A genus of mitosporic fungi containing about 100 species and eleven different teleomorphs in the family Trichocomaceae.
D001236	Aspergillus oryzae	An imperfect fungus present on most agricultural seeds and often responsible for the spoilage of seeds in bulk storage. It is also used in the production of fermented food or drink, especially in Japan.	Eurotium oryzae
D013379	Substrate Specificity	A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.	Specificities, Substrate,Specificity, Substrate,Substrate Specificities