Proteinases of Legionella: phenylalanineaminopeptidase of L. pneumophila.
Phenylalanineaminopeptidase was isolated and purified from the culture filtrate of Legionella pneumophila by affinity chromatography on O-tert-butyl-L-threonyl-L-phenylalanyl-L-prolylglycyl-aminosilo chrom and by gel-filtration; a 401-fold purification with a yield of 18% was achieved. The enzyme was a metalloenzyme with a molecular weight of 35000 and a pI of 5.8. It was stable at pH 7-9 and had an activity optimum in the range of pH 8-9.5 with L-phenylalanine p-nitroanilide as substrate. Enzyme activity was highest towards the latter compound, substantially lower towards L-leucine p-nitroanilide and only marginal towards other p-nitroanilides. Besides phenylalanineaminopeptidase, a metalloproteinase and a serine proteinase were also detected in L. pneumophila culture filtrate.
Gul'nik
S V
SV
Yusupova
M P
MP
Lavrenova
G I
GI
Tartakovsky
I S
IS
Prozorovsky
S V
SV
Stepanov
V M
VM
D000596:Amino Acids / Q000032:analysis; D000626:Aminopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007875:Legionella / Q000201:enzymology*
D000596:Amino Acids; D000626:Aminopeptidases; C049035:phenylalanine aminopeptidase