title: Regulation of the secretion of Rhizopus oligosporus extracellular carboxyl proteinase.
abstract: Secretion of the extracellular Rhizopus carboxyl proteinase (EC 3.4.23.6) by Rhizopus oligosporus is repressed in the presence of low-molecular-mass sources of nitrogen, sulphur and carbon. Proteinase is secreted when the medium is deficient in any one of these three nutrients. In the case of nitrogen metabolite repression, control is at the level of transcription. Induction of proteinase secretion by exogenous protein does not occur in any of the media examined.
authors: Fakultas Biologi, Universitas Kristen Satya Wacana, Salatiga, Indonesia.
authors: P C
authors: PC
authors: Farley
authors: L
authors: L
authors: Ikasari
mesh_terms: D016282:Aspartic Acid Endopeptidases / Q000378:metabolism*; D001483:Base Sequence; D002244:Carbon / Q000378:metabolism; D003470:Culture Media; D004794:Enzyme Repression; D008969:Molecular Sequence Data; D009584:Nitrogen / Q000378:metabolism; D012233:Rhizopus / Q000201:enzymology*; D013455:Sulfur / Q000378:metabolism
chemical_list: D003470:Culture Media; D013455:Sulfur; D002244:Carbon; D016282:Aspartic Acid Endopeptidases; C035794:rhizopuspepsin; D009584:Nitrogen