The large family of peptide-bond-cleaving hydrolases, the peptidases () proteases, EC 3.4),
can be categorized as endopeptidases () proteinases, EC 3.4. 21-99) and exopeptidases …

Cysteinyl proteinases and their selective inactivation Page 281 CYSTEINYL PROTEINASES
AND THEIR SELECTIVE INACTIVATION By ELLIOTT SHAW, Friedrich Miescher-Institut …

Amide bond formation is one of the most important reactions in both chemistry and biology,,–
, but there is currently no chemical method of achieving α-peptide ligation in water that …

Papain is a sulfhydryl protease from the latex of the papaya fruit. Its molecules consist of one
polypeptide chain with 212 amino acid residues. The chain is folded into two domains with …

Mature viral-encoded proteins of tobacco etch virus (TEV) arise by proteolytic processing of
a large precursor. The proteinase responsible for most of these cleavages is a viral-encoded …

The structure of the sulphydryl protease, actinidin, after refinement at 1.7 Å resolution, is
described. The positions of most of the 1666 atoms have been determined with an accuracy …

Posttranslational modification of proteins with ubiquitin and ubiquitin-like modifiers such as
SUMO can be reverted by specific proteases, also referred to as deubiquitinases and …

Serine proteinases are among the most exten-sively studied enzymes (for recent reviews
see Blow, 1976; Kraut, 1977; Huber & Bode, 1978). Their best known representatives, like …

The cysteine proteinases form a group of enzymes which depend for their activity on the thiol
group of a cysteine residue. They occur in mammals plants and bacteria and fulfil a wide …

Aldehydes, structurally related to the acyl portion of substrates, are extremely potent
competitive inhibitors of papain. At pH 5.5 and 25°, approximately 1 mole of acetyl-l …