Homologous inhibitors from potato tubers of serine endopeptidases and metallocarboxypeptidases. [PDF]
Proceedings of the National Academy of Sciences, 1976 A potent polypeptide inhibitor of chymotrypsin has been purified from Russett Burbank potatoes. The inhibitor has no effect on bovine carboxypeptidases A or B but exhibits homology with a carboxypeptidase inhibitor that is also present in potato tubers.
Claus HASS +2 more
semanticscholar +5 more sources
Self Purification of Two Serine Endopeptidases [PDF]
Proceedings of the National Academy of Sciences, 1972 We have reported that a serine protease from Pronase, homologous with bovine chymotrypsin, is both active and stable in 6 M guanidinium chloride. The present investigation examined the possibility that this unique property might be used to permit the enzyme to engage in its own purification by cleaving companion proteins to low-molecular ...
William M. Awad +2 more
semanticscholar +4 more sources
Discovery and biochemical characterization of the D-aspartyl endopeptidase activity of the serine protease LACTB. [PDF]
J Biol ChemNon-enzymatic D-isomerization of aspartic acid in proteins has been observed in lesions associated with age-related diseases, including cataracts and Alzheimer's disease. Given that D-isomerization of Asp disrupts the physiological conformation of proteins, it has been postulated that D-isomerization of Asp in proteins is a key factor in the ...
Ito G, Utsunomiya-Tate N.
europepmc +4 more sources
Insights into the efficient degradation mechanism of extracellular proteases mediated by Purpureocillium lilacinum [PDF]
Frontiers in MicrobiologyProtease secretion is crucial for degrading nematode cuticles using nematophagous fungus Purpureocillium lilacinum, but the secretion pattern of protease remains poorly understood.
Xiujun Zhang +7 more
doaj +3 more sources
FEBS Letters, 1988 Subunit III (BSIII) of the bovine ternary complex of procarboxypeptidase A‐S6 (PCPA‐S6), a defective serine endopeptidase‐like protein, actively synthesized by the pancreas of some ruminant species, is highly homologous to human protease E (HPE). Both proteins possess the same atypical disulfide bridge in position 98–99b.
Christian Cambillau +3 more
semanticscholar +4 more sources
Genetic Biodiversity and Posttranslational Modifications of Protease Serine Endopeptidase in Different Strains of Sordaria fimicola [PDF]
BioMed Research International, 2023 Genetic variations (mutation, crossing over, and recombination) act as a source for the gradual alternation in phenotype along a geographic transect where the environment changes. Posttranslational modifications (PTMs) predicted modifications successfully in different and the same species of living organisms.
Uzma Naureen +5 more
openalex +3 more sources
Immunoglobulin A protease from Sutterella wadsworthensis modifies outcome of infection with Campylobacter jejuni and is associated with microbiome diversity [PDF]
Gut MicrobesSutterella wadsworthensis is an enigmatic member of the microbiota, previously reported to be present in healthy humans yet also associated with certain gut diseases and their therapeutic outcomes. Here, we report on S.
Marwan E. Majzoub +6 more
doaj +2 more sources
Substrate Specificity of Honeydew Melon Protease D, a Plant Serine Endopeptidase [PDF]
Bioscience, Biotechnology, and Biochemistry, 1997 The substrate specificity of honeydew melon (Cucumis melo var. inodorus Naud) protease D was studied by the use of synthetic substrates and oligopeptides derived from a protein hydrolyzate. The hydrolysis rates of succinyl-(L-Ala)1-3-p-nitroanilide (Suc-(Ala)1-3-pNA) the hydrolysis rate progressively rose in proportion to the increased chain length ...
Hiroo Yonezawa +2 more
openalex +4 more sources
Action of serine carboxypeptidases on endopeptidase substrates, peptide‐4‐methyl‐coumaryl‐7‐amides [PDF]
European Journal of Biochemistry, 1985 Carboxypeptidase Y hydrolyzed N‐substituted peptide‐4‐methylcoumarin‐7‐amides (peptide‐NH‐Mec) at pH 7 by releasing 7‐amino‐4‐methylcoumarin (NH2‐Mec) which was then followed by carboxypeptidase action. In particular, a chymotrypsin‐directed substrate, Suc‐Leu‐Leu‐Val‐Tyr‐NH‐Mec, was hydrolyzed by the enzyme with a second‐order rate constant of 7200 ...
Shigeru Kunugi +2 more
openalex +3 more sources
Modeling and structural analysis of PA clan serine proteases
BMC Research Notes, 2012 Background Serine proteases account for over a third of all known proteolytic enzymes; they are involved in a variety of physiological processes and are classified into clans sharing structural homology. The PA clan of endopeptidases is the most abundant
Laskar Aparna +3 more
doaj +2 more sources