Results 141 to 150 of about 4,257 (183)

Structure modeling of a metalloendopeptidase from Corynebacterium pseudotuberculosis

Computers in Biology and Medicine, 2012
Metalloendopeptidases 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 ...
Luis Guimarães, Natália F. Silva, Anderson Miyoshi, Maria P. C. Schneider, Artur Silva, Vasco Ariston de Carvalho Azevedo, Davi S. B. Brasil, Jerônimo Lameira, Cláudio Nahum Alves   +8 more
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Biological markers in pneumoconioses : plasma metalloendopeptidase and matrix metalloendopeptidase

1991
The 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, El Nabout, R., Oberson, Dominique, Auburtin, Guy, Gillet, Chantal, Sebastien, Patrick, Lafuma, C.   +6 more
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Membrane Metalloendopeptidases in Immune Function and Disease

1997
The enzymes that compose the ‘Metallopeptidases’ are a diverse group1. Forty-seven distinct evolutionary families of metallopeptidases have been identified in the last eight years; more than for any other protease classes, i.e., the serine/threonine, cysteine, or aspartic classes of proteases (see the Peptidase World Wide Web sites:http://www.qmw.ac.uk/
J S, Bond, W, Jiang
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Substrate-related potent inhibitors of brain metalloendopeptidase

Biochemistry, 1988
Rat brain metalloendopeptidase (EC 3.4.24.15) generates Leu- and Met-enkephalin from several larger opioid peptides and is capable of degrading a number of neuropeptides. Substrate-related N-(1-carboxy-3-phenylpropyl) peptide derivatives were synthesized and tested for enzyme inhibition.
M, Orlowski, C, Michaud, C J, Molineaux
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Degradation of bradykinin by a metalloendopeptidase from Streptococcus pyogenes

Journal of Oral Biosciences, 2016
Streptococcus pyogenes secretes streptococcal pyrogenic exotoxin B (SpeB), which cleaves kininogen to liberate bradykinin. In addition, this bacterium also has cell-associated bradykinin-degrading activity. Here, we characterized the bradykinin-degrading enzyme produced by S.
Yoichi, Miyamoto, Takaaki, Akaike, Shigetada, Kawabata, Teruo, Akuta, Chiho, Taruki, Jun, Yoshitake, Shigeyuki, Hamada, Fusao, Ota, Hideo, Igarashi, Kentaro, Yoshimura, Ryutaro, Kamijo, Hiroshi, Maeda   +11 more
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Features of gene expression of Bacillus pumilus metalloendopeptidase

Biochemistry (Moscow), 2016
Features 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.
Rudakova N., Sabirova A., Balaban N., Tikhonova A., Sharipova M.   +4 more
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Structural aspects of the metzincin clan of metalloendopeptidases

Molecular Biotechnology, 2003
Metalloendopeptidases are present across all kingdoms of living organisms; they are ubiquitous and widely involved in metabolism regulation through their ability either to extensively degrade proteins or to selectively hydrolyze specific peptide bonds. They must be subjected to exquisite spatial and temporal control to prevent this vast potential from ...
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Metalloendopeptidase EC 3.4.24.15 in Neurodegeneration

2002
The metalloendopeptidases represent a fascinating class of enzymes involved in neurodegenerative diseases. Many metalloendopeptidases are integrally involved in brain processes. This family boasts enkephalinase (24.11), neurolysin (24.16), and others.
Carmela R. Abraham, Franchot Slot
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Peptidyl-Asp metalloendopeptidase.

Methods in enzymology, 1995
M L, Hagmann, U, Geuss, S, Fischer, G B, Kresse   +3 more
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Metalloendopeptidase activity in urine of rodents.

Biomedica biochimica acta, 1992
The brush border membrane of mice and rats contains a phosphoramidon-insensitive metalloproteinase, meprin (neutral endopeptidase-2; NEP-2). The role of meprin is unknown, but we have shown that urine from these species contains insulin B chain degrading activity that is due to a phosphoramidon-insensitive metalloendopeptidase.
R J, Beynon, A V, Flannery, G C, Macadam
openaire   +1 more source