Proteolytic processing of neuropeptide Y and peptide YY by dipeptidyl peptidase IV
R Mentlein, P Dahms, D Grandt, R Krüger - Regulatory peptides, 1993 - Elsevier
Neuropeptide Y, peptide YY and pancreatic polypeptide share an evolutionary conserved
proline-rich N-terminal sequence, a structure generally known to be inert to the attack of
common proteinases, but a potential target for specialized proline-specific aminopeptidases.
Purified human dipeptidyl peptidase IV (also termed CD 26) liberated N-terminal Tyr-Pro
from both, neuropeptide Y and peptide YY, with very high specific activities and K m values
in the micromolar range, but almost no Ala-Pro from pancreatic polypeptide. Other proline …
proline-rich N-terminal sequence, a structure generally known to be inert to the attack of
common proteinases, but a potential target for specialized proline-specific aminopeptidases.
Purified human dipeptidyl peptidase IV (also termed CD 26) liberated N-terminal Tyr-Pro
from both, neuropeptide Y and peptide YY, with very high specific activities and K m values
in the micromolar range, but almost no Ala-Pro from pancreatic polypeptide. Other proline …