Results 171 to 180 of about 5,868 (229)

Insect carboxypeptidases

open access: yes, 2013
The third edition of the Handbook of Proteolytic Enzymes aims to be a comprehensive reference work for the enzymes that cleave proteins and peptides, and contains over 850 chapters. Each chapter is organized into sections describing the name and history, activity and specificity, structural chemistry, preparation, biological aspects, and distinguishing
John A. Gatehouse, Gatehouse, J.A.
openaire   +3 more sources

Trichophyton rubrum secreted and membrane-associated carboxypeptidases

open access: yesInternational Journal of Medical Microbiology, 2008
Dermatophytes are the most common agents of superficial mycoses, and exclusively infect stratum corneum, nails or hair. Therefore, secreted proteolytic activity is considered a virulence trait of these fungi.
Christophe Zaugg   +2 more
exaly   +2 more sources

Carboxypeptidases

open access: yes, 1999
Josep Vendrell, Francesc X. Avilés
openaire   +2 more sources

Cellular carboxypeptidases

Immunological Reviews, 1998
Summary: This article focuses on four human carboxypeptidases (CPs): two metallo‐CPs and two serine CPs. The metallo‐CPs are members of the so‐called B‐type regulatory CP family, as they cleave only the C‐terminal basic amino acids Arg or Lys. The plasma membrane‐bound CPM and the mainly, but not exclusively, intracellular CPD are surveyed from this ...
R A, Skidgel, E G, Erdös
openaire   +2 more sources

Cleavage of the carboxypeptidase inhibitor from potatoes by carboxypeptidase A

Biochemical and Biophysical Research Communications, 1980
Summary The association of carboxypeptidase A with the carboxypeptidase inhibitor from potatoes results in the rapid removal of the carboxyl-terminal glycine residue from the inhibitor. At an equimolar concentration of inhibitor and enzyme, the half-time for hydrolysis is approximately thirty seconds at pH 7.5.
G M, Hass, C A, Ryan
openaire   +2 more sources

Carboxypeptidase E

Annual Review of Physiology, 1988
Carboxypeptidase E appears to be involved in the biosynthesis of a wide range of peptide hormones and neurotransmitters. The evidence for this is: (a) CPE is present in tissues that produce bioactive peptides; (b) in tissues that have been subjected to subcellular fractionation, the CPE activity is associated with peptide-containing secretory granules;
openaire   +2 more sources

Dynamical structure of carboxypeptidase A

Journal of Molecular Biology, 1989
Structural fluctuations of the apoenzyme form of carboxypeptidase A (EC 3.4.12.2) have been evaluated on the basis of molecular dynamics. The Konnert-Hendrickson refined coordinates of 2437 non-hydrogen atoms of the 307 amino acid residues derived from the X-ray structure of the holoenzyme served as the molecular model together with 548 calculated ...
MAKINEN, MW   +4 more
openaire   +3 more sources

Studies on Carboxypeptidase A

1974
In this article the main theme to be discussed will be our continuing studies on the mechanism of action of the zinc-containing metalloenzyme bovine carboxypeptidase A. A summary of earlier mechanistic studies in our laboratory on carboxypeptidase A was published recently (Kaiser and Kaiser, 1972).
E T, Kaiser, T W, Chan, J, Suh
openaire   +2 more sources

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