Purification and characterization of L-phenylalanine aminopeptidase from chick-pea cotyledons (Cicer arietinum L.).
Chick-pea (Cicer arietinum L.) cotyledons are unique source of aminopeptidase - 8-9 U/g cotyledons was observed using L-leucine-p-nitroanilide as substrate. The aminopeptidase was purified (65 kDa, pI 4.8 ) reaching a specific activity of 220 U/mg at pH 7.0-7.2 and 35-40 degrees C. The determined constant of specificity k(cat)/K(m) during hydrolysis of N-unsubstituted amino acid-p-nitroanilides showed a decrease order: Phe>Leu>Pro>Ile>Val>Ala. The enzyme was strongly inhibited by p-chloromercuribenzoic acid as well as in a competitive rate by the antihypertensive peptides Ile-Pro-Pro and Val-Pro-Pro.
Marinova
Margarita
M
Institute of Organic Chemistry with Centre of Phytochemistry, Bulgarian Academy of Sciences, Acad. G. Bonchev Str. 9, 1113 Sofia, Bulgaria.
Dolashki
Alexander
A
Altenberend
Florian
F
Stevanovic
Stefan
S
Voelter
Wolfgang
W
Tchorbanov
Bozhidar
B
D000626:Aminopeptidases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D029863:Cicer / Q000201:enzymology*; D018548:Cotyledon / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D009842:Oligopeptides / Q000378:metabolism; D016415:Sequence Alignment; D013379:Substrate Specificity; D013696:Temperature
D009842:Oligopeptides; C489032:isoleucyl-prolyl-proline; C489031:valyl-prolyl-proline; D000626:Aminopeptidases; C049035:phenylalanine aminopeptidase