Results 111 to 120 of about 4,088 (165)
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The novel ADAMs-like microbial metalloendopeptidase
Russian Journal of Bioorganic Chemistry, 2012Heterologous gene expression of extracellular minor metalloendopeptidase of Bacillus pumilus 3-19 in protease-deficient B. subtilis strain has been studied. The fraction of enzyme in total pool of B. pumilus 3-19 secreted proteases composes less than 8%.
Sharipova M R
exaly +5 more sources
Features of gene expression of Bacillus pumilus metalloendopeptidase
Biochemistry (Moscow), 2016Features of gene expression of the secreted Bacillus pumilus metalloendopeptidase belonging to the adamalysin/reprolysin family were investigated. In the regulatory region of the gene, we identified hypothetical binding sites for transcription factors CcpA and TnrA.
Sharipova M R
exaly +5 more sources
Structure modeling of a metalloendopeptidase from Corynebacterium pseudotuberculosis
Computers in Biology and Medicine, 2012Metalloendopeptidases are zinc-dependent hydrolases enzymes with many different roles in biological systems, ranging from remodeling conjunctive tissue to removing signaling sequences from nascent proteins. Here, we describe the three-dimensional structure of the metalloendopeptidase from Corynebacterium pseudotuberculosis generated by homology ...
, Jeronimo Lameira, Anderson Miyoshi
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Extracellular metalloendopeptidase of Streptomyces rimosus
Archives of Microbiology, 2006Metalloendopeptidase was isolated from Streptomyces rimosus culture filtrates in a homogeneous form. It was determined to be a 15 kDa basic protein, most active around pH 7.5, and susceptible to inhibition by chelating agents, N-bromosuccinimide, thiorphan, and 10(-4) M zinc. The enzyme was highly specific for phenylalanine at the N-side of endopeptide
Vitale, Ljubinka +2 more
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ADAM10, myelin-associated metalloendopeptidase
2004The subject of this chapter is ADAM10, myelin-associated metalloendopeptidase. ADAM10 is a zinc-dependent metallo-endopeptidase with a C-terminal distintegrin domain. It is a homolog of adamalysin. As an α-secretase, it is protective against Alzheimer’s disease, cleaving the Aβ protein so that the damaging β-secretase cleavage is reduced.
Postina, Rolf, Fahrenholz, Falk
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New metalloendopeptidase of Morganella morganii ZM
Russian Journal of Bioorganic Chemistry, 2014Proteolytic activity which is inhibited in the presence of o-phenanthroline was found in M. morganii ZM. Intracellular proteases of M. morganii ZM unlimited split musculoskeletal actin in contrast to grimelysin. Several proteolitic proteins of M. morganii ZM cells were identified by zymography with gelatin. Metalloproteinase of M.
Zamaliutdinova N. +3 more
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Inhibition of metalloendopeptidases by 2‐mercaptoacetyl‐dipeptides
European Journal of Biochemistry, 1983A series of 2‐mercaptoacetyl‐dipeptides, a potential group of metalloendopeptidase inhibitors, has been synthesized by coupling the N‐hydroxysuccinimide ester of S‐acetyl‐2‐mercaptoacetic acid with hydrophobic dipeptide methyl ester hydrochlorides, followed by hydrolysis with NaOH in aqueous methanol and acidification with HCl.
S, Blumberg, Z, Tauber
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Biological markers in pneumoconioses : plasma metalloendopeptidase and matrix metalloendopeptidase
1991The design and validation ofbiomarkers can contribute significantly to early detection of biological effects and identification ofthose who are at risk ofcoal workers' pneumoconiosis (CWP). This research is designed to evaluate diflerent plasma metalloendopeptidase and metalloproteinase activities to estimate harmfui exposure in coalminers from ...
Porcher, Jean-Marc +6 more
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Action of neutral metalloendopeptidase (“enkephalinase”) on β-endorphin
Neuropeptides, 1985Human beta-endorphin was digested by neutral metalloendopeptidase from rabbit kidney and the products were isolated and identified. Based on the structure and yield of the fragments, the major cleavage sites were identified with the Leu17-Phe18, Gly3-Phe4, Pro13-Leu14 and Ile22-Ile23 peptide bonds of the beta-endorphin structure.
L, Gráf, A, Páldi, A, Patthy
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