Completing the acylation landscape in plants: GDSL enzymes join the BAHD and SCPL acyltransferase families. [PDF]
J Exp BotMallavergne A, Hilbert JL, Gagneul D.
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The bradykinin B2 receptor as a context-dependent modulator of neural circuit function. [PDF]
Front Cell NeurosciSilva JLS +3 more
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Real-time FRET assay for monitoring detyrosination by TMCP1 and VASH2. [PDF]
Protein SciSimon M +5 more
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Metalation of Extracytoplasmic Proteins and Bacterial Cell Envelope Homeostasis. [PDF]
Annu Rev MicrobiolHe B, Helmann JD.
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Microbial fermentation of soybeans: synergistic enhancement of bioactivity and sensory properties. [PDF]
Food Chem XGong R, Zalán Z, Song J, Suo H.
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The Effects of Adding Walnut Green Husk on the Quality of Alfalfa Mixed Silage, Protein Degradation, Microbial Community, and Their Interrelationships. [PDF]
MetabolitesAbulaiti N, Aiyisirehong G, Yimamu A.
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Trichophyton rubrum secreted and membrane-associated carboxypeptidases
International 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.
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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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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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