title: Specificity of acid protease from Fusarium moniliforme.
abstract: Specificity of acid protease from Fusarium moniliforme was investigated using beta chain of oxidized insulin. The enzyme is highly specific for the bonds involving aromatic and hydrophobic amino acid residues. It shows high affinity for the following bonds: Leu(15)-Tyr(16), Tyr(16)-Leu(17), Phe(24)-Phe(25), Phe(25)-Tyr(26), and somewhat lower for other three bonds: His(10)-Leu(11), Leu(11)-Val(12) and Tyr(26)-Thr(27) in oxidized beta chain of insulin.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000378:metabolism; D016282:Aspartic Acid Endopeptidases; D003619:Dansyl Compounds / Q000032:analysis; D010450:Endopeptidases / Q000032:analysis / Q000378:metabolism*; D005670:Fusarium / Q000201:enzymology*; D010455:Peptides / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D000596:Amino Acids; D003619:Dansyl Compounds; D010455:Peptides; D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases