Serine carboxypeptidases. A review
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چکیده
منابع مشابه
Organ-specific and hormone-dependent expression of genes for serine carboxypeptidases during development and following germination of rice grains.
Several cDNA clones encoding either serine carboxypeptidases or related proteins of Oryza sativa L. were identified, and the abundance of the corresponding mRNA in immature and germinated grains was examined. The deduced amino acid sequence of each cDNA included key sequences, such as a pentapeptide (G-X-S-X-G/A) that is conserved among many serine carboxypeptidases, and the putative protein pr...
متن کاملPeptide inhibitors of Streptomyces DD-carboxypeptidases.
1. Peptides that inhibit the dd-carboxypeptidases from Streptomyces strains albus G and R61 were synthesized. They are close analogues of the substrates of these enzymes. The enzymes from albus G and R61 strains are in general inhibited by the same peptides, but the enzyme from strain R39 differs considerably. 2. The two C-terminal residues of the peptide substrates and inhibitors appear to be ...
متن کاملMice, double deficient in lysosomal serine carboxypeptidases Scpep1 and Cathepsin A develop the hyperproliferative vesicular corneal dystrophy and hypertrophic skin thickenings
Vasoactive and mitogenic peptide, endothelin-1 (ET-1) plays an important role in physiology of the ocular tissues by regulating the growth of corneal epithelial cells and maintaining the hemodynamics of intraocular fluids. We have previously established that ET-1 can be degraded in vivo by two lysosomal/secreted serine carboxypeptidases, Cathepsin A (CathA) and Serine Carboxypeptidase 1 (Scpep1...
متن کاملTranspeptidase activity of Streptomyces D-alanyl-D carboxypeptidases.
In the presence of N(alpha),N(epsilon)-diacetyl-L-Lys-D-Ala-D-Ala as donor, and either D-[(14)C]alanine, [(14)C]-glycine, or meso-[(3)H]diaminopimelic acid as acceptor, the DD carboxypeptidases from Streptomyces R61 and R39 catalyze a transpeptidation reaction with the release of terminal D-alanine from the donor and the formation of either N(alpha),N(epsilon)-diacetyl-L-Lys-D-Ala-D-[(14)C]Ala,...
متن کاملPurification and characterization of two serine carboxypeptidases from Aspergillus niger and their use in C-terminal sequencing of proteins and peptide synthesis.
A procedure was developed to prepare in large amounts two carboxypeptidases, CPD-I and CPD-II, from Aspergillus niger. They were each shown to be serine proteases and single-chain monomers with molecular masses of ca. 81 kDa and containing 22% carbohydrates. Amino acid analysis, carbohydrate determination, and N-terminal sequencing (20 to 25 residues) were performed on each enzyme. CPD-I showed...
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ژورنال
عنوان ژورنال: Carlsberg Research Communications
سال: 1986
ISSN: 0105-1938
DOI: 10.1007/bf02907561