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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
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Production and application of peptidyl-lys metalloendopeptidase: advances, challenges, and future perspectives [PDF]
Applied Microbiology and BiotechnologyPeptidyl-lys metalloendopeptidases (PKMs) are enzymes that selectively cleave peptide bonds at the N-terminus of lysine residues present in the P1′ position, making them valuable tools in proteomics.
Uzair Ahmed +2 more
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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.
Robert Beynon, J S Bond
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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 ...
J S Bond
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Chromosome-level genome assembly of the nematophagous flatworm Luticola nematophagus: revealing molecular adaptations for predation and its biocontrol potential against nematode diseases [PDF]
BMC GenomicsBackground The soil-dwelling Rhabdocoela flatworm, Luticola nematophagus, recently identified as a specialized predator of plant-parasitic nematodes such as Meloidogyne incognita, demonstrates considerable potential as a biocontrol agent for agricultural
Chongtao Guo +10 more
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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 ...
Rebecca A Lew, A Ian Smith
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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.
Barrett A J
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The ADAMTS family: from extracellular matrix proteases to orchestrators of fibrosis [PDF]
Cell Communication and SignalingFibrosis, a pathological process defined by excessive extracellular matrix (ECM) accumulation, contributes significantly to chronic organ failure worldwide.
Yang Yuan +4 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
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Journal of Oral Biology and Craniofacial Research, 2023 Salivary gland (SG) extracellular matrix (ECM) has a major influence on tissue development, homeostasis, and tissue regeneration after injury. During aging, disease, and physical insult, normal remodeling of the SG microenvironment (i.e.
Milos Marinkovic +6 more
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