[Isolation and properties of serine proteinase from Aspergillus oryzae].
A serine proteinase having an activity optimum at pH 6.7-8.2 has been isolated from amylorisine P-10x (a mixture of Aspergillus oryzae enzymes) by chromatography on DEAE-Sephadex A-50 and bacitracin Sepharose 4B. The proteinase is fully inactivated by phenylmethylsulfonylfluoride and diisopropylfluorophosphonate, the specific inhibitors of the enzyme, and has a pI at pH 7.5. The molecular mass of serine proteinase is 30000 Da; its amino acid composition appears as: Met2, Asp33, Thr18, Ser29, Glu21, Pro9, Glu32, Ala38, Val24, Ile16, Leu15, Tyr8, Phe8, His8, Lys18, Arg4, Trp6. The N-terminal sequence of the serine proteinase: Gly-Leu-Thr-Thr-Gln-Lys-Ser-Ala-Pro-Trp-Gly-Leu-Gly-Ser-Ile-Ser-Xaa-Lys- Gly-Gln-Gln-Ser-Thr-Asp-Tyr-Ile-Tyr, which coincides practically completely with the corresponding sequence of alkaline proteinase of A. oryzae, ATCC20386, has been determined. Similar to subtilisin, the enzyme catalyzes the condensation of leucine and alanine p-nitroanilides with N-benzyloxycarbonyl-alanyl-alanine and glycyl-alanine methyl esters.
Vagonova
T I
TI
Ivanova
N M
NM
Khodova
O M
OM
Voiushina
T L
TL
Stepanov
V M
VM
D000595:Amino Acid Sequence; D001236:Aspergillus oryzae / Q000201:enzymology*; D002850:Chromatography, Gel; D006863:Hydrogen-Ion Concentration; D007531:Isoflurophate / Q000494:pharmacology; D008969:Molecular Sequence Data; D010664:Phenylmethylsulfonyl Fluoride / Q000494:pharmacology; D012697:Serine Endopeptidases / Q000737:chemistry / Q000302:isolation & purification*; D015842:Serine Proteinase Inhibitors
D015842:Serine Proteinase Inhibitors; D007531:Isoflurophate; D010664:Phenylmethylsulfonyl Fluoride; D012697:Serine Endopeptidases
Vydelenie i svoĭstva serinovoĭ proteinazy aspergillus oryzae.