Isolation and characterization of a dipeptidyl aminopeptidase from Streptomyces sp. WM-23.
A screening test was undertaken to isolate microorganisms that produced dipeptidyl aminopeptidase. The hydrolytic activity toward alanyl-phenylalanine p-nitroanilide was found in a culture filtrate of a actinomyces strain (WM-23), newly isolated from a soil sample. The enzyme (WM-23 dipeptidyl aminopeptidase) was isolated from the culture filtrate as a homogeneous preparation. The WM-23 enzyme, inhibited by phenylmethylsulfonyl fluoride, may be classified to mammalian dipeptidyl aminopeptidase II. The enzymatic characteristics were investigated.
Murao
S
S
Department of Applied Microbial Technology, Kumamoto Institute of Technology, Japan.
Kitade
T
T
Oyama
H
H
Shin
T
T
D000595:Amino Acid Sequence; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D008970:Molecular Weight; D013302:Streptomyces / Q000201:enzymology*
D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases