排列5往期中奖号码:Aspartate Protease & Regulator-enzyme

12097期排列5 www.ixpcv.com Aspartic proteases are a group of protease enzymes that use two highly conserved aspartic acid residues in the active site for catalytic cleavage of their peptide substrates. Unlike serine or cysteine proteases these proteases do not form a covalent intermediate during cleavage. Nearly all known aspartyl proteases are inhibited by pepstatin. HIV protease is unusual in that it is a homodimer and each of the monomeric units contribute an aspartic acid.

As the smallest class, aspartic proteases nevertheless play an important role in health and disease. For example, beta-secretase are the two enzymes necessary to release A beta peptides from the Alzheimer's precursor protein. BACE1 and Cathepsin D & E all have beta secretase activity and Presenilin is the catalytic subunit of the gamma secretase complex that contains three other integral membrane proteins. As a general protease inhibitor, alpha 2-Macroglobulin is able to inhibit all four classes of proteases by a unique trapping mechanism.

Cathepsin
CTSD/Cathepsin D CTSE/Cathepsin E
Pepsinogen
PGC/Pepsinogen C PGA4/Pepsinogen A4
Renin
Renin/Ren Renin R/ATP6AP2
Secretase / Presenilin
APH1A PSEN1 CD147/EMMPRIN/Basigin
Nicastrin/NCSTN TMP21/TMED10  
BACE/Beta-secretase
BACE1/Beta-secretase 1 BACE2/Beta secretase 2
Aspartic Protease Regulators
A2M/alpha-2-macroglobulin PZP/Pregnancy Zone Protein
Renin R/ATP6AP2 ITM2B
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