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The astacin family of metalloendopeptidases [PDF]
Protein Science, 1995 AbstractThe astacin family of metalloendopeptidases was recognized as a novel family of proteases in the 1990s. The crayfish enzyme astacin was the first characterized and is one of the smallest members of the family. More than 20 members of the family have now been identified.
J S, Bond, R J, Beynon
semanticscholar +5 more sources
Identification and bioinformatic analysis of neprilysin and neprilysin-like metalloendopeptidases in <i>Drosophila melanogaster</i>. [PDF]
MicroPubl Biol, 2021 The neprilysin (M13) family of metalloendopeptidases comprises highly conserved ectoenzymes that cleave and thereby inactivate many physiologically relevant peptides in the extracellular space.
Meyer H +5 more
europepmc +5 more sources
Homologues of insulinase, a new superfamily of metalloendopeptidases [PDF]
Biochemical Journal, 1991 On the basis of a statistical analysis of an alignment of the amino acid sequences, a new superfamily of metalloendopeptidases is proposed, consisting of human insulinase, Escherichia coli protease III and mitochondrial processing endopeptidases from Saccharomyces and Neurospora.
N D, Rawlings, A J, Barrett
semanticscholar +5 more sources
Natural Inhibitors of Snake Venom Metalloendopeptidases: History and Current Challenges
Toxins, 2016 The research on natural snake venom metalloendopeptidase inhibitors (SVMPIs) began in the 18th century with the pioneering work of Fontana on the resistance that vipers exhibited to their own venom.
Viviane A. Bastos +4 more
doaj +2 more sources
It Takes Two to Tango: Current Understanding of the Role of M16 Family of Proteases and Their Structural Properties [PDF]
BiomoleculesThe M16 protease family comprises metalloendopeptidases, characterized by a unique molecular architecture. The active enzyme molecule is composed of two halves, which together form a structure resembling a clam shell.
Miroslaw Jarzab, Joanna Skorko-Glonek
doaj +2 more sources
Soluble Metalloendopeptidases and Neuroendocrine Signaling [PDF]
Endocrine Reviews, 2002 Peptidases play a vital and often highly specific role in the physiological and pathological generation and termination of peptide hormone signals. The thermolysin-like family of metalloendopeptidases involved in the extracellular processing of neuroendocrine and cardiovascular peptides are of particular significance, reflecting both their specificity ...
Corie N, Shrimpton +2 more
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Commitment to expression of the metalloendopeptidases, collagenase and stromelysin: relationship of inducing events to changes in cytoskeletal architecture [PDF]
Journal of Cell Biology, 1986 Agents that alter the morphology of rabbit synovial fibroblasts induce synthesis of the metalloendopeptidases, collagenase and stromelysin. We studied the relationship of cytoskeletal changes to the commitment to expression of these metalloendopeptidases.
Z. Werb +3 more
semanticscholar +2 more sources
Families of metalloendopeptidases and their relationships [PDF]
FEBS Letters, 1992 Crystal structures available for four metalloendopeptidases have revealed zinc ligands for these enzymes. New sequence information has made it possible to compare the primary structures of the zinc‐binding site in metalloendopeptidases. A scheme based on the zinc‐binding site is proposed to classify metalloendopeptidases into five distinct families ...
Jiang, Weiping, Bond, Judith S.
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Secretion of Metalloendopeptidase 24.15 (EC 3.4.24.15) [PDF]
DNA and Cell Biology, 1999 The metalloendopeptidase EP24.15 (EC3.4.24.15) is a neuropeptide-metabolizing enzyme present in neural and endocrine tissues, presumably functioning extracellularly. Because the majority of the EP24.15 activity is identified in the soluble fraction of cellular homogenates, suggesting that the enzyme is primarily an intracellular protein, we addressed ...
Ferro, E. S. +3 more
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The astacin family of metalloendopeptidases.
Journal of Biological Chemistry, 1991 Molecular cloning of a human intestinal brush border metalloendopeptidase (N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase, PPH) and a mouse kidney brush border metalloendopeptidase (meprin A) has revealed 82% identity in the NH2-terminal amino acid sequences (198 residues) of the mature enzymes.
E, Dumermuth +6 more
openaire +3 more sources