Article
Human meprin beta: O-linked glycans in the intervening region of the type I membrane protein protect the C-terminal region from proteolytic cleavage and diminish its secretion.
The Biochemical journal - 1 Feb 2003
Leuenberger Boris, Hahn Dagmar, Pischitzis Anastassios, Hansen Marianne K, Sterchi Erwin E
Abstract excerpt
Human meprin (hmeprin; N -benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase; EC 3.4.24.18) is a member of the astacin family of zinc metalloendopeptidases. The major site of expression is the brush border membrane of small intestinal and kidney epithelial cells. The enzyme is a type I integral membrane protein composed of two distinct subunits, alpha and beta, which are linked by disulphide bridges. The enzyme...
Topics
- Acetylgalactosamine
- Amino Acid Sequence
- Animals
- Benzyl Compounds
- Carbohydrate Conformation
- Caseins
- Cells, Cultured
- Glycosylation
- Humans
- Membrane Proteins
- Metalloendopeptidases
- Molecular Sequence Data
- Mutation