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CELA3B chymotrypsin-like elastase family, member 3B

proproteinase E, procarboxypeptidase A-S6 subunit III
Top mentioned proteins: elastase, carboxypeptidase, Trypsin, Chymotrypsin, OUT
Papers on proproteinase E
Cutting at the right place--the importance of selective limited proteolysis in the activation of proproteinase E.
Avilés et al., Barcelona, Spain. In Eur J Biochem, 1998
Its proform from the bovine pancreatic system has been structurally analyzed by X-ray crystallography for the intact native form, with a 11-residue N-terminal activation peptide, in a ternary complex with chymotrypsinogen C and procarboxypeptidase A [Gomis-Rüth, F. X., Gómez, M., Bode, W., Huber, R. & Avilés, F. X. (1995) The three-dimensional structure of the native ternary complex of bovine pancreatic procarboxypeptidase A with proproteinase E and chymotrypsinogen C, EMBO J. 14, 4387-4394].
Crystal structure of an oligomer of proteolytic zymogens: detailed conformational analysis of the bovine ternary complex and implications for their activation.
Avilés et al., Barcelona, Spain. In J Mol Biol, 1997
In this heterotrimeric complex, the 403 residue procarboxypeptidase A takes a central position, with chymotrypsinogen C and proproteinase E attached to different surface sites of it.
How to escape from model bias with a high-resolution native data set - structure determination of the PcpA-S6 subunit III.
Wilson et al., Grenoble, France. In Acta Crystallogr D Biol Crystallogr, 1996
The structure of procarboxypeptidase A-S6 subunit III, a truncated zymogen E, has been determined by molecular replacement using as search model porcine elastase 1 which, as revealed by crystallographic analysis, contained about 20% of the amino acids in a radically different orientation.
The three-dimensional structure of the native ternary complex of bovine pancreatic procarboxypeptidase A with proproteinase E and chymotrypsinogen C.
Avilés et al., Barcelona, Spain. In Embo J, 1995
The metalloexozymogen procarboxypeptidase A is mainly secreted in ruminants as a ternary complex with zymogens of two serine endoproteinases, chymotrypsinogen C and proproteinase E. The bovine complex has been crystallized, and its molecular structure analysed and refined at 2.6 A resolution to an R factor of 0.198.
Crystallographic study of a cleaved, non-activatable form of porcine zymogen E.
Fontecilla-Camps et al., Grenoble, France. In J Mol Biol, 1995
The crystal structure of a cleaved form of porcine zymogen E has been solved by molecular replacement using the bovine procarboxypeptidase A-S6 subunit III structure as search model.
Crystallization and preliminary X-ray analysis of the ternary complex of procarboxypeptidase A from bovine pancreas.
Avilés et al., Barcelona, Spain. In Febs Lett, 1995
The ternary complex of procarboxypeptidase A, chymotrypsinogen C and proproteinase E from bovine pancreas has been crystallized using the sitting drop vapour diffusion method.
Crystal structure of bovine procarboxypeptidase A-S6 subunit III, a highly structured truncated zymogen E.
Fontecilla-Camps et al., Grenoble, France. In Embo J, 1994
Subunit III, a defective serine endopeptidase lacking the typical N-terminal hydrophobic dipeptide is secreted by the pancreas of ruminant species as part of the bovine ternary complex procarboxypeptidase A-S6.
Autolysis of proproteinase E in bovine procarboxypeptidase A ternary complex gives rise to subunit III.
Puigserver et al., Barcelona, Spain. In Febs Lett, 1991
Extracts of bovine pancreatic tissue are shown by HPLC to contain two distinct ternary complexes of procarboxypeptidase A (subunit I), chymotrypsinogen C (subunit II) and either proproteinase E or subunit III.
The separation of pancreatic procarboxypeptidases by high-performance liquid chromatography and chromatofocusing.
Avilés et al., Barcelona, Spain. In J Chromatogr, 1989
The sequential use of gel filtration (or anion-exchange) and reversed-phase HPLC chromatography permitted, in a simple way, the isolation and dissociation of the strongly bound components of the binary complexes between procarboxypeptidases A and proproteinase E in either porcine or human pancreas extracts.
Generation of a subunit III-like protein by autolysis of human and porcine proproteinase e in a binary complex with procarboxypeptidase A.
Puigserver et al., Barcelona, Spain. In Biochem Biophys Res Commun, 1989
Tryptic treatment of human and porcine proproteinase E, procarboxypeptidase A binary complexes gave rise to active proteinase E after removal of an 11-residue N-terminal activation peptide.
Purification and properties of five different forms of human procarboxypeptidases.
Aviles et al., Barcelona, Spain. In Eur J Biochem, 1989
Two of the procarboxypeptidases A, the A1 and A2 forms, are obtained in a monomeric state while the other, the A3 form, is obtained as a binary complex of a procarboxypeptidase A with a proproteinase E. This complex is stable in aqueous buffers at various ionic strengths and develops carboxypeptidase A and proteinase E activities in the presence of trypsin.
Urea-gradient gel electrophoresis studies on the association of procarboxypeptidases A and B, proproteinase E, and their tryptic activation products.
Avilés et al., In Febs Lett, 1985
Monomeric procarboxypeptidase A (PCPA) and isolated proproteinase E (PPE), both from pig pancreas, were shown by means of electrophoresis on transverse urea gradients (0-9 M) to form a very stable complex, identical to their natural binary complex.
Sequential homologies between procarboxypeptidases A and B from porcine pancreas.
Méndez et al., In Biochem Biophys Res Commun, 1985
On the other hand, tryptic peptide maps on a reverse-phase column indicate great sequential similarities (if not identity) between monomeric procarboxypeptidase A and the procarboxypeptidase A subunit isolated from its binary complex with proproteinase E.
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