Results 1 to 10 of about 6,236 (183)
Journal of Basic and Applied ZoologyBackground Sicarius rugosus, the only member of the genus that inhabits Central America, is phylogenetically related to South American Sicarius spiders. These originated from a common ancestor with sister African species.
Cecilia Díaz +3 more
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CARBOXYPEPTIDASE, A ZINC METALLOENZYME
Journal of Biological Chemistry, 1955 B L, VALLEE, H, NEURATH
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Studies on Catheptic Carboxypeptidase
Journal of Biological Chemistry, 1962 L M, GREENBAUM, R, SHERMAN
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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
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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
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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;
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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;
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Cleavage of the carboxypeptidase inhibitor from potatoes by carboxypeptidase A
Biochemical and Biophysical Research Communications, 1980Summary 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
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Dynamical structure of carboxypeptidase A
Journal of Molecular Biology, 1989Structural 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
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